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1,4-beta-D-mannan + H2O
?
2,4-dinitrophenyl-beta-mannobioside + H2O
2,4-dinitrophenol + beta-mannobiose
-
-
-
-
?
4-methylumbelliferyl mannotrioside + H2O
4-methylumbelliferone + mannotriose
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
aesculin + H2O
aesculetin + D-glucose
-
-
-
-
?
azo-carob galactomannan + H2O
?
azurine-crosslinked galactomannan + H2O
?
-
hydrolysis
-
-
?
beta-1,4-D-mannan + H2O
?
166% of the activity with locust bean gum
main products are manno-oligosaccharides of 2-6 residues and mannose
-
?
beta-1,4-mannan + H2O
?
-
-
-
?
beta-1,4-mannan + H2O
beta-1,4-mannotriose + beta-1,4-mannotetraose
-
-
-
-
?
beta-1,4-mannan + H2O
mannobiose + mannotriose
-
-
-
?
beta-1,4-mannan + H2O
mannose + mannobiose + mannotriose
87% activity compared to konjac glucomannan
-
-
?
beta-galactomannan + H2O
mannobiose + mannotriose + mannotetraose
-
the catalytic efficiency of the enzyme is 6.8fold higher toward galactomannan from locust bean gum, than toward galactomannan from guar gum, but similar toward galactomannan from locust bean gum and glucomannan from konjac flour
-
-
?
beta-glucomannan + H2O
mannobiose + mannotriose + mannotetraose
-
the catalytic efficiency of the enzyme is 6.8fold higher toward galactomannan from locust bean gum, than toward galactomannan from guar gum, but similar toward galactomannan from locust bean gum and glucomannan from konjac flour
-
-
?
beta-mannan + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
carob galactomannan + H2O
?
carob glucomannan + H2O
?
carob-galactomannan + H2O
?
i.e. locust bean gum
-
-
?
cellulose + H2O
?
-
-
-
-
?
ceratonia siliqua gum + H2O
?
-
46.6% activity compared to locust bean gum
-
-
?
copra mannan + H2O
?
-
90% of the activity with locust bean gum
-
-
?
copra meal defatted with n-hexane + H2O
?
defatted copra meal + H2O
?
fenugreek gum + H2O
?
-
268.1% activity compared to locust bean gum
-
-
?
galactoglucomannan + H2O
?
galactoglucomannan + oligosaccharide
[3H]-labelled polysaccharide
-
transglucosylation
-
-
?
galactomannan + H2O
galactosyl-mannosyl oligosaccharides
galactomannan + H2O
hydrolyzed galactomannan
galactomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose
-
different contents of glucose and mannose, overview
product ratio overview
-
?
Gelatin + H2O
?
-
-
-
-
?
glucomannan + H2O
glucosyl-mannosyl oligosaccharides
glucomannan + H2O
mannobiose + mannotriose
high activity
-
-
?
glucomannan + H2O
oligosaccharides
guar galactomannan + H2O
?
guar gum + H2O
mannobiose + mannotriose
-
-
mannobiose, mannotriose, and a mixture of various mannose-linked oligosaccharides
-
?
guar gum + H2O
mannobiose + mannotriose + mannose
guar gum + H2O
mannose + mannobiose + mannotriose
guar gum + H2O
mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose
-
-
product ratio overview
-
?
guar gum galactomannan + H2O
?
guar gum glucomannan + H2O
?
insoluble mannan + H2O
mannotriose + mannotetraose + mannopentaose
ivory nut mannan + H2O
mannobiose + mannotriose
ivory nut mannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
-
-
-
-
?
ivory nut mannan + H2O
mannotriose + mannotetraose + mannopentaose + mannohexaose
konjac glucomannan + H2O
?
konjac glucomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
konjac powder + H2O
?
33.5% activity compared to locust bean gum
-
-
?
konjac powder + H2O
mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose + mannoheptaose
-
85.1% activity compared to locust bean gum
-
-
?
konjaku flour + H2O
mannobiose + mannotriose + mannose
locust bean galactomannan + H2O
mannotriose + mannotetraose + mannopentaose
locust bean gum + H2O
mannobiose + mannotriose
locust bean gum + H2O
mannobiose + mannotriose + mannotetraose
locust bean gum + H2O
mannopentaose
locust bean gum + H2O
mannose + ?
locust bean gum + H2O
mannose + galactose
locust bean gum + H2O
mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose
-
-
product ratio overview
-
?
locust bean gum + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
-
-
-
-
?
locust bean gum + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose + mannoheptaose
-
100% activity
-
-
?
locust bean gum + H2O
mannotriose + ?
locust bean gum galactomannan + H2O
?
highest activity
-
-
?
locust bean gum galactomannan + H2O
mannobiose + glucosyl-mannosyl oligosaccharides
-
main product, with low amounts of mannotriose and higher manno-oligosaccharides
-
?
locust bean gum galactomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
locust bean gum glucomannan + H2O
?
low viscosity locust bean galactomannan + H2O
?
-
-
-
-
?
low-viscosity locust bean galactomannan + H2O
?
-
-
-
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
2 Man-beta-1,4-Man
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
Man-beta-1,4-Man-beta-1,4-Man + Man-beta-1,4-Man
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
Man-beta-1,4-Man + Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Manbeta(1-4)Manbeta(1-4)Man + H2O
?
-
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Man + H2O
mannose + Manbeta(1-4)Man
-
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
?
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + mannose
-
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + mannose + Manbeta(1-4)Man
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
mannose + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Man
-
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + mannose
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + mannose
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man-ol + H2O
D-mannitol + Manbeta(1-4)Man-ol + D-mannose + Manbeta(1-4)Manbeta(1-4)Man-ol + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man-ol + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man-ol + Manbeta(1-4)Manbeta(1-4)Man
-
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man-ol + H2O
Manbeta(1-4)Man-ol + Manbeta(1-4)Manbeta(1-4)Man + mannose + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man-ol + Manbeta(1-4)Man
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + mannose
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Man + mannose + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
-
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man-ol + H2O
mannose + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man-ol + Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man-ol + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
-
-
-
?
mannan + H2O
mannosyl oligosaccharides
-
products show a degree of polymerization of 2-6
-
?
mannan + H2O
mannotetraose + mannobiose + mannotriose
mannan + H2O
oligosaccharides
mannan A + H2O
?
-
-
-
-
?
mannobiose + H2O
mannose + mannobiose
-
degradation of mannobiose yields a mixture of mannose (16.6 %) and mannobiose (83.4 %)
-
-
?
mannohexaose + H2O
2 mannotriose
-
-
main product
-
?
mannohexaose + H2O
mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannohexaose + H2O
mannotriose + mannotetraose + mannopentaose + mannobiose
-
-
-
?
mannopentaose + H2O
mannobiose + mannotriose
-
-
-
-
?
mannopentaose + H2O
mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose
-
degradation of mannopentaose yields a mixture of mannose (3.1 %), mannobiose (11.2 %), mannotriose (41.1%), mannotetraose (21.7%), and mannopentaose (22.9%)
-
-
?
mannopentaose + H2O
mannose + mannotetraose
-
-
-
?
mannopentaose + H2O
mannotetraose + ?
-
-
-
?
mannopentaose + H2O
mannotriose + mannobiose
-
-
main products
-
?
mannopentaose + H2O
mannotriose + mannobiose + mannotetraose
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
mannotetraose + H2O
mannobiose + mannotriose + mannopentaose
-
-
-
?
mannotetraose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
degradation of mannotetraose yields a mixture of mannose (2.4 %), mannobiose (9.5 %) and mannotriose (62.3%) and mannotetraose (25.8%)
-
-
?
mannotetraose + H2O
mannotriose + mannobiose
-
-
-
?
mannotriose + H2O
mannobiose + mannose
mannotriose + H2O
mannose + mannobiose + mannotriose
-
degradation of mannotriose yields a mixture of mannose (2.8 %), mannobiose (11.8 %) and mannotriose (85.4%)
-
-
?
sesbania gum + H2O
?
-
26% activity compared to konjac glucomannan
-
-
?
sodium phytate + H2O
?
-
-
-
-
?
soluble mannan + H2O
mannosyl oligosaccharides
-
-
-
-
?
tara gum + H2O
?
-
galactose-mannose ratio of 1:3
-
-
?
tara gum galactomannan + H2O
?
-
-
-
-
?
xanthan gum + H2O
mannose + mannobiose
-
345.6% activity compared to locust bean gum
-
-
?
additional information
?
-
1,4-beta-D-mannan + H2O
?
-
-
-
?
1,4-beta-D-mannan + H2O
?
-
-
-
?
1,4-beta-D-mannan + H2O
?
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
-
-
-
?
azo-carob galactomannan + H2O
?
-
-
-
?
azo-carob galactomannan + H2O
?
-
-
-
?
birch wood xylan + H2O
?
9.1% of the activity with locust bean gum
-
-
?
birch wood xylan + H2O
?
9.1% of the activity with locust bean gum
-
-
?
carboxymethyl cellulose + H2O
?
-
poor substrate
-
-
?
carboxymethyl cellulose + H2O
?
-
poor substrate
-
-
?
carob galactomannan + H2O
?
-
-
-
?
carob galactomannan + H2O
?
56% activity compared to konjac glucomannan
-
-
?
carob galactomannan + H2O
?
-
-
-
?
carob glucomannan + H2O
?
13% of the activity with konjac glucomannan
-
-
?
carob glucomannan + H2O
?
13% of the activity with konjac glucomannan
-
-
?
carrageenan gum + H2O
?
-
71% activity compared to locust bean gum
-
-
?
carrageenan gum + H2O
?
-
71% activity compared to locust bean gum
-
-
?
copra meal defatted with n-hexane + H2O
?
-
better substrate than locust bean gum and guar gum
-
-
?
copra meal defatted with n-hexane + H2O
?
-
better substrate than locust bean gum and guar gum
-
-
?
defatted copra meal + H2O
?
-
-
-
-
?
defatted copra meal + H2O
?
-
-
-
-
?
galactoglucomannan + H2O
?
-
-
-
-
?
galactoglucomannan + H2O
?
-
-
-
-
?
galactoglucomannan + H2O
?
-
-
-
-
?
galactoglucomannan + H2O
?
-
-
-
-
?
galactoglucomannan + H2O
?
-
-
-
-
?
galactoglucomannan + H2O
?
-
-
-
-
?
galactoglucomannan + H2O
?
-
-
-
-
?
galactoglucomannan + H2O
?
-
-
-
-
?
galactoglucomannan + H2O
?
-
-
-
-
?
galactoglucomannan + H2O
?
-
-
-
-
?
galactomannan + H2O
?
-
-
-
?
galactomannan + H2O
?
-
-
-
-
?
galactomannan + H2O
?
-
-
-
-
?
galactomannan + H2O
?
-
-
-
-
?
galactomannan + H2O
?
-
-
-
?
galactomannan + H2O
?
-
the enzyme exhibits higher activity on galactomannan branched with (1->6)-linked alpha-D-galactose than glucomannan
-
-
?
galactomannan + H2O
?
-
-
-
?
galactomannan + H2O
?
-
the enzyme exhibits higher activity on galactomannan branched with (1->6)-linked alpha-D-galactose than glucomannan
-
-
?
galactomannan + H2O
?
-
-
-
?
galactomannan + H2O
?
-
-
-
-
?
galactomannan + H2O
galactosyl-mannosyl oligosaccharides
-
source of substrate locust bean gum
-
-
?
galactomannan + H2O
galactosyl-mannosyl oligosaccharides
-
products show a degree of polymerization of 2-6
-
?
galactomannan + H2O
galactosyl-mannosyl oligosaccharides
-
enzyme prefers galactomannans with lower degree of galactosylation e.g. from carob gum
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
-
-
-
-
?
glucomannan + H2O
?
-
-
-
?
glucomannan + H2O
?
-
-
-
?
glucomannan + H2O
?
219% of the activity with locust bean gum
-
-
?
glucomannan + H2O
?
-
-
-
-
?
glucomannan + H2O
?
-
from konjac flour
products are a large amount of oligosaccharides with a degree of polymerizytion of 2-6 and a very small amount of monosaccharide
-
?
glucomannan + H2O
?
-
from konjac flour
products are a large amount of oligosaccharides with a degree of polymerizytion of 2-6 and a very small amount of monosaccharide
-
?
glucomannan + H2O
?
-
-
-
-
?
glucomannan + H2O
?
-
-
-
-
?
glucomannan + H2O
?
-
-
-
?
glucomannan + H2O
?
from konjac flour
-
-
?
glucomannan + H2O
?
-
-
-
-
?
glucomannan + H2O
?
from konjac flour
70% of the activity with locust bean gum
-
?
glucomannan + H2O
?
-
-
-
?
glucomannan + H2O
?
-
highest activity
-
-
?
glucomannan + H2O
?
from konjac flour
-
-
?
glucomannan + H2O
?
from konjac flour
-
-
?
glucomannan + H2O
glucosyl-mannosyl oligosaccharides
-
source of substrate konjac
-
-
?
glucomannan + H2O
glucosyl-mannosyl oligosaccharides
-
products show a degree of polymerization of 2-6
-
?
glucomannan + H2O
oligosaccharides
-
-
of various size
?
glucomannan + H2O
oligosaccharides
-
-
-
-
?
glucomannan + H2O
oligosaccharides
-
-
-
-
?
glucomannan + H2O
oligosaccharides
-
-
-
-
?
glucomannan + H2O
oligosaccharides
-
-
-
-
?
glucomannan + H2O
oligosaccharides
-
-
-
-
?
glucomannan + H2O
oligosaccharides
-
-
-
-
?
glucomannan + H2O
oligosaccharides
-
-
-
-
?
glucomannan + H2O
oligosaccharides
-
-
-
-
?
glucomannan + H2O
oligosaccharides
Lilium testaceum
-
-
-
-
?
glucomannan + H2O
oligosaccharides
-
-
-
-
?
glucomannan + H2O
oligosaccharides
-
-
-
?
glucomannan + H2O
oligosaccharides
Tyromyces palustris
-
-
of various size
?
glucomannan + H2O
oligosaccharides
-
-
-
?
glucomannan + H2O
oligosaccharides
-
-
-
?
guar galactomannan + H2O
?
1.4% of the activity with konjac glucomannan
-
-
?
guar galactomannan + H2O
?
1.4% of the activity with konjac glucomannan
-
-
?
guar gum + H2O
?
highest activity with a mannose to galactose ratio of 79:21
-
-
?
guar gum + H2O
?
-
18.1% activity compared to konjac glucomannan
-
-
?
guar gum + H2O
?
-
18.1% activity compared to konjac glucomannan
-
-
?
guar gum + H2O
?
-
-
-
-
?
guar gum + H2O
?
-
-
-
-
?
guar gum + H2O
?
-
41.2% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
-
41.2% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
-
-
-
-
?
guar gum + H2O
?
18% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
-
90% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
18% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
-
galactose-mannose ratio of 2:3
-
-
?
guar gum + H2O
?
-
highest activity
-
-
?
guar gum + H2O
?
-
21% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
-
350% activity compared to locust bean gum
-
-
?
guar gum + H2O
?
-
21% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
-
350% activity compared to locust bean gum
-
-
?
guar gum + H2O
?
-
14.8% of the activity with locust bean gum
-
?
guar gum + H2O
?
-
-
-
-
?
guar gum + H2O
?
12.2% activity compared to locust bean gum
-
-
?
guar gum + H2O
?
-
-
-
-
?
guar gum + H2O
?
-
26% of the activity with locust bean gum
-
?
guar gum + H2O
?
-
26% of the activity with locust bean gum
-
?
guar gum + H2O
?
-
-
-
-
?
guar gum + H2O
?
-
-
-
-
?
guar gum + H2O
?
-
-
-
-
?
guar gum + H2O
?
-
1.7% activity compared to konjac glucomannan
-
-
?
guar gum + H2O
mannobiose + mannotriose + mannose
-
-
-
?
guar gum + H2O
mannobiose + mannotriose + mannose
-
-
-
?
guar gum + H2O
mannose + mannobiose + mannotriose
-
-
-
?
guar gum + H2O
mannose + mannobiose + mannotriose
-
-
mannobiose + mannotriose + mannotetraose
?
guar gum + H2O
mannose + mannobiose + mannotriose
-
-
-
?
guar gum + H2O
mannose + mannobiose + mannotriose
-
-
-
?
guar gum + H2O
mannose + mannobiose + mannotriose
Penicillium wortmanni
-
-
-
?
guar gum + H2O
mannose + mannobiose + mannotriose
-
-
-
?
guar gum galactomannan + H2O
?
-
-
-
-
?
guar gum galactomannan + H2O
?
-
-
-
?
guar gum glucomannan + H2O
?
-
-
-
?
guar gum glucomannan + H2O
?
-
-
-
?
insoluble mannan + H2O
mannotriose + mannotetraose + mannopentaose
-
-
-
-
?
insoluble mannan + H2O
mannotriose + mannotetraose + mannopentaose
-
-
-
-
?
ivory nut mannan + H2O
?
moderate activity
-
-
?
ivory nut mannan + H2O
?
-
-
-
?
ivory nut mannan + H2O
?
-
-
-
?
ivory nut mannan + H2O
?
-
-
-
?
ivory nut mannan + H2O
?
-
lowest activity
-
-
?
ivory nut mannan + H2O
?
-
lowest activity
-
-
?
ivory nut mannan + H2O
?
-
-
-
-
?
ivory nut mannan + H2O
?
-
46% activity compared to konjac glucomannan
-
-
?
ivory nut mannan + H2O
mannobiose + mannotriose
-
-
-
?
ivory nut mannan + H2O
mannobiose + mannotriose
-
-
-
?
ivory nut mannan + H2O
mannotriose + mannotetraose + mannopentaose + mannohexaose
-
main products, at 14%, 25%, 20%, and 13%, respectively
-
?
ivory nut mannan + H2O
mannotriose + mannotetraose + mannopentaose + mannohexaose
-
main products, at 14%, 25%, 20%, and 13%, respectively
-
?
konjac flour + H2O
?
high activity
-
-
?
konjac flour + H2O
?
-
-
-
-
?
konjac glucomannan + H2O
?
-
100% activity
-
-
?
konjac glucomannan + H2O
?
-
100% activity
-
-
?
konjac glucomannan + H2O
?
-
-
-
-
?
konjac glucomannan + H2O
?
-
-
-
?
konjac glucomannan + H2O
?
-
-
-
?
konjac glucomannan + H2O
?
100% activity
-
-
?
konjac glucomannan + H2O
?
-
highest activity
-
-
?
konjac glucomannan + H2O
?
-
highest activity
-
-
?
konjac glucomannan + H2O
?
-
-
-
?
konjac glucomannan + H2O
?
-
-
-
?
konjac glucomannan + H2O
?
-
-
-
?
konjac glucomannan + H2O
?
-
highest activity
-
-
?
konjac glucomannan + H2O
?
-
highest activity
-
-
?
konjac glucomannan + H2O
?
-
-
-
?
konjac glucomannan + H2O
?
-
-
-
?
konjac glucomannan + H2O
?
-
-
-
-
?
konjac glucomannan + H2O
?
-
best substrate
-
-
?
konjac glucomannan + H2O
?
-
-
-
?
konjac glucomannan + H2O
?
-
-
-
?
konjac glucomannan + H2O
?
-
-
-
?
konjac glucomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
-
-
-
-
?
konjac glucomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
-
-
-
-
?
konjaku flour + H2O
mannobiose + mannotriose + mannose
-
-
-
?
konjaku flour + H2O
mannobiose + mannotriose + mannose
-
-
-
?
locust bean galactomannan + H2O
mannotriose + mannotetraose + mannopentaose
-
-
-
-
?
locust bean galactomannan + H2O
mannotriose + mannotetraose + mannopentaose
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
?
locust bean gum + H2O
?
-
88.2% activity compared to konjac glucomannan
-
-
?
locust bean gum + H2O
?
-
88.2% activity compared to konjac glucomannan
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
galactose-mannose ratio of 1:4
-
-
?
locust bean gum + H2O
?
-
-
-
?
locust bean gum + H2O
?
-
main products are manno-oligosaccharides of 2-6 residues and mannose
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
?
locust bean gum + H2O
?
-
products are various manno-oligosaccharides of M2-M6 size and mannose
-
?
locust bean gum + H2O
?
-
enzyme is highly specific for substrate
-
-
?
locust bean gum + H2O
?
-
enzyme is highly specific for substrate
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
?
locust bean gum + H2O
?
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
?
locust bean gum + H2O
?
100% activity
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
76% of products are oligomannosides
-
?
locust bean gum + H2O
?
-
hydrolysis products are mainly oligosaccharides plus one monosaccharide
-
?
locust bean gum + H2O
?
-
hydrolysis products are mainly oligosaccharides plus one monosaccharide
-
?
locust bean gum + H2O
?
-
76% of products are oligomannosides
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
?
locust bean gum + H2O
?
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
?
locust bean gum + H2O
?
-
9.6% activity compared to konjac glucomannan
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
-
?
locust bean gum + H2O
?
-
-
-
?
locust bean gum + H2O
?
-
-
-
?
locust bean gum + H2O
?
-
-
-
?
locust bean gum + H2O
?
-
-
-
?
locust bean gum + H2O
mannobiose + mannotriose
-
52.7% mannobiose, 18.1% mannotriose and 29.2% other unidentifiable oligosaccharides
-
?
locust bean gum + H2O
mannobiose + mannotriose
-
52.7% mannobiose, 18.1% mannotriose and 29.2% other unidentifiable oligosaccharides
-
?
locust bean gum + H2O
mannobiose + mannotriose
-
best substrate
mannobiose, mannotriose, and a mixture of various mannose-linked oligosaccharides
-
?
locust bean gum + H2O
mannobiose + mannotriose + mannotetraose
-
best substrate
hydrolysis products are 17.2% mannobiose, 37.4% mannotriose, 9.9% mannotetraose, and 35.5% other unidentified oligosaccharides
-
?
locust bean gum + H2O
mannobiose + mannotriose + mannotetraose
-
best substrate
hydrolysis products are 17.2% mannobiose, 37.4% mannotriose, 9.9% mannotetraose, and 35.5% other unidentified oligosaccharides
-
?
locust bean gum + H2O
mannobiose + mannotriose + mannotetraose
-
-
-
?
locust bean gum + H2O
mannopentaose
-
44%, main product
-
?
locust bean gum + H2O
mannopentaose
-
44%, main product
-
?
locust bean gum + H2O
mannose + ?
-
highest activity
-
-
?
locust bean gum + H2O
mannose + ?
-
-
-
-
?
locust bean gum + H2O
mannose + ?
-
-
-
-
?
locust bean gum + H2O
mannose + galactose
-
-
-
-
?
locust bean gum + H2O
mannose + galactose
-
-
-
-
?
locust bean gum + H2O
mannose + galactose
-
-
-
-
?
locust bean gum + H2O
mannose + galactose
-
-
-
?
locust bean gum + H2O
mannose + galactose
-
-
-
?
locust bean gum + H2O
mannotriose + ?
-
-
-
?
locust bean gum + H2O
mannotriose + ?
-
-
-
?
locust bean gum galactomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
-
-
-
-
?
locust bean gum galactomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
-
-
-
-
?
locust bean gum glucomannan + H2O
?
-
-
-
?
locust bean gum glucomannan + H2O
?
-
-
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
2 Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4 mannooligosaccharides with the degree of polymerisation from 4 to 6
64% of product
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
2 Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4-mannooligosaccharides with the degree of polymerisation from 4 to 6
68% of product
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
2 Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4-mannooligosaccharides with the degree of polymerisation from 4 to 6
68% of product
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
2 Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4 mannooligosaccharides with the degree of polymerisation from 4 to 6
64% of product
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
Man-beta-1,4-Man-beta-1,4-Man + Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4 mannooligosaccharides with the degree of polymerisation from 4 to 6
sole products
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
Man-beta-1,4-Man-beta-1,4-Man + Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4-mannooligosaccharides with the degree of polymerisation from 4 to 6
sole products
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
Man-beta-1,4-Man + Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4 mannooligosaccharides with the degree of polymerisation from 4 to 6
88% of products
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
Man-beta-1,4-Man + Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4-mannooligosaccharides with the degree of polymerisation from 4 to 6
88% of products
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + mannose
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + mannose
-
-
-
?
mannan + H2O
?
the amino-terminal catalytic domain has beta-mannanase activity, and the carboxy-terminal domain acts as an endoglucanase
-
-
?
mannan + H2O
mannotetraose + mannobiose + mannotriose
-
source of substrate: copra
-
-
?
mannan + H2O
mannotetraose + mannobiose + mannotriose
-
source of substrate: copra
-
-
?
mannan + H2O
oligosaccharides
-
codium, coffee
-
-
?
mannan + H2O
oligosaccharides
-
-
dimers, trimers and other
?
mannan + H2O
oligosaccharides
-
-
dimers, trimers and other
?
mannan + H2O
oligosaccharides
-
-
-
-
?
mannan + H2O
oligosaccharides
-
-
-
-
?
mannan + H2O
oligosaccharides
-
-
-
?
mannan + H2O
oligosaccharides
-
-
-
-
?
mannan + H2O
oligosaccharides
-
-
-
?
mannan + H2O
oligosaccharides
-
-
-
?
mannan + H2O
oligosaccharides
-
-
-
-
?
mannan + H2O
oligosaccharides
-
-
dimers, trimers and other
?
mannan + H2O
oligosaccharides
-
-
-
-
?
mannan + H2O
oligosaccharides
-
-
-
-
?
mannan + H2O
oligosaccharides
-
-
-
-
?
mannan + H2O
oligosaccharides
-
-
-
-
?
mannan + H2O
oligosaccharides
-
-
dimers, trimers and other
?
mannan + H2O
oligosaccharides
-
-
dimers, trimers and other
?
mannan + H2O
oligosaccharides
Penicillium wortmanni
-
-
dimers, trimers and other
?
mannan + H2O
oligosaccharides
-
-
-
?
mannan + H2O
oligosaccharides
-
-
dimers, trimers and other
?
mannan + H2O
oligosaccharides
-
-
dimers, trimers and other
?
mannan + H2O
oligosaccharides
-
-
-
?
mannan + H2O
oligosaccharides
-
-
-
-
?
mannan + H2O
oligosaccharides
-
-
-
?
mannan + H2O
oligosaccharides
-
-
-
-
?
mannohexaose + H2O
?
-
-
-
?
mannohexaose + H2O
?
-
-
-
-
?
mannohexaose + H2O
?
-
-
-
?
mannopentaose + H2O
?
-
-
-
?
mannopentaose + H2O
?
-
-
-
-
?
mannopentaose + H2O
?
-
-
-
-
?
mannopentaose + H2O
?
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
?
mannotetraose + H2O
?
-
-
-
-
?
mannotetraose + H2O
?
-
-
-
-
?
mannotetraose + H2O
?
-
-
-
-
?
mannotetraose + H2O
?
-
-
-
-
?
mannotetraose + H2O
?
-
-
-
-
?
mannotetraose + H2O
?
-
-
-
-
?
mannotetraose + H2O
?
the wild-type enzyme produces mannobiose as dominant product from mannotetraose. The R171K mutant enzyme produces mannotriose and mannose
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
small amounts of mannose and mannotriose
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
small amounts of mannose and mannotriose
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
small amounts of mannose and mannotriose
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
-
-
?
mannotriose + H2O
?
-
-
-
-
?
mannotriose + H2O
?
-
-
-
-
?
mannotriose + H2O
?
-
-
-
?
mannotriose + H2O
mannobiose + mannose
-
-
-
?
mannotriose + H2O
mannobiose + mannose
-
-
-
?
mannotriose + H2O
mannobiose + mannose
-
-
-
?
mannotriose + H2O
mannobiose + mannose
-
-
not
?
palm kernel cake + H2O
?
-
-
-
-
?
palm kernel cake + H2O
?
-
-
-
-
?
starch + H2O
?
-
-
-
-
?
starch + H2O
?
-
poor substrate
-
-
?
starch + H2O
?
-
poor substrate
-
-
?
xylan + H2O
?
-
poor substrate
-
-
?
xylan + H2O
?
-
poor substrate
-
-
?
additional information
?
-
-
production of mannooligosaccharides from pretreated and defatted copra meal hydrolysis by the enzyme
-
-
?
additional information
?
-
-
production of mannooligosaccharides from pretreated and defatted copra meal hydrolysis by the enzyme
-
-
?
additional information
?
-
-
not: mannobiose
-
-
?
additional information
?
-
no activity with mannotriose, barley beta-glucan, birchwood xylan, and carboxymethyl cellulose
-
-
?
additional information
?
-
-
the enzyme shows no activity towards carboxymethyl cellulose, xylan, glucan, pectin, chitin, soluble starch, or alpha-1,6-linked yeast mannan. Also, the enzyme shows no activity on 4-nitrophenyl beta- and alpha-mannosides, beta- and alpha-galactosides, and beta- and alpha-glucosides
-
-
?
additional information
?
-
-
the enzyme shows no activity towards carboxymethyl cellulose, xylan, glucan, pectin, chitin, soluble starch, or alpha-1,6-linked yeast mannan. Also, the enzyme shows no activity on 4-nitrophenyl beta- and alpha-mannosides, beta- and alpha-galactosides, and beta- and alpha-glucosides
-
-
?
additional information
?
-
-
preferably degrades a linear beta-1,4-mannan from green algae Codium fragile producing tri- and disaccharides. no substrate: carboxymethyl cellulose, agarose, dextran and xylan
-
-
?
additional information
?
-
-
the enzyme is involved in release of mannooligosaccharides from spent coffee ground cleaving the backbone at random locations in galactomannan, glucomannan, galactoglucomannan and mannan
-
-
?
additional information
?
-
-
the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides
-
-
?
additional information
?
-
-
the enzyme has no exo-activity and is a typical endo-acting beta-mannanase, substrate specificity, overview. No activity with mannobiose, beechwood xylan, barley beta-glucan, 4-nitrophenyl beta-D-mannoside, and carboxymethyl cellulose
-
-
?
additional information
?
-
-
the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides
-
-
?
additional information
?
-
-
the enzyme has no exo-activity and is a typical endo-acting beta-mannanase, substrate specificity, overview. No activity with mannobiose, beechwood xylan, barley beta-glucan, 4-nitrophenyl beta-D-mannoside, and carboxymethyl cellulose
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
enzyme displays good transgycosylation activity using mannotriose, melezitose and isomaltotriose as acceptors
-
-
?
additional information
?
-
enzyme displays good transgycosylation activity using mannotriose, melezitose and isomaltotriose as acceptors
-
-
?
additional information
?
-
enzyme displays transglycosylation activity using only mannotriose as acceptor
-
-
?
additional information
?
-
enzyme displays transglycosylation activity using only mannotriose as acceptor
-
-
?
additional information
?
-
-
no activity with beechwood xylan, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-mannoside, and carboxymethyl cellulose
-
-
?
additional information
?
-
enzyme displays good transgycosylation activity using mannotriose, melezitose and isomaltotriose as acceptors
-
-
?
additional information
?
-
enzyme displays good transgycosylation activity using mannotriose, melezitose and isomaltotriose as acceptors
-
-
?
additional information
?
-
enzyme displays transglycosylation activity using only mannotriose as acceptor
-
-
?
additional information
?
-
enzyme displays transglycosylation activity using only mannotriose as acceptor
-
-
?
additional information
?
-
-
no activity with beechwood xylan, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-mannoside, and carboxymethyl cellulose
-
-
?
additional information
?
-
-
not: mannobiose
-
-
?
additional information
?
-
-
not: mannobiose
-
-
?
additional information
?
-
negligible activity with starch, carboxymethyl cellulose, and alpha-cellulose
-
-
?
additional information
?
-
-
negligible activity with starch, carboxymethyl cellulose, and alpha-cellulose
-
-
?
additional information
?
-
negligible activity with starch, carboxymethyl cellulose, and alpha-cellulose
-
-
?
additional information
?
-
-
negligible activity with starch, carboxymethyl cellulose, and alpha-cellulose
-
-
?
additional information
?
-
-
no activity with mannobiose, mannotriose, and mannotetraose
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
not: mannobiose
-
-
?
additional information
?
-
-
no activity with cellulose, casein and pectin
-
-
?
additional information
?
-
the enzyme does not show activity toward guar galactomannan, 4-nitrophenyl beta-D-mannopyranoside, mannobiose, birchwood xylan, or carboxymethyl cellulose
-
-
?
additional information
?
-
-
no substrate: carboxymethyl cellulose
-
-
?
additional information
?
-
no substrates: mannobiose, mannotriose, mannotetraose, mannohexaose
-
-
?
additional information
?
-
-
no substrates: mannobiose, mannotriose, mannotetraose, mannohexaose
-
-
?
additional information
?
-
no substrate: guar gum, copra meal
-
-
?
additional information
?
-
-
no activity on starch and xylan
-
-
?
additional information
?
-
-
no substrate: carboxymethyl cellulose
-
-
?
additional information
?
-
-
no activity on starch and xylan
-
-
?
additional information
?
-
-
the enzyme displays no activity towards mannotriose, Avicel and guar gum
-
-
?
additional information
?
-
-
the enzyme displays no activity towards mannotriose, Avicel and guar gum
-
-
?
additional information
?
-
no substrate: mannobiose, or 4-nitrophenyl sugar derivatives
-
-
?
additional information
?
-
no substrate: mannobiose, or 4-nitrophenyl sugar derivatives
-
-
?
additional information
?
-
-
no substrate: mannotriose, mannobiose, enzyme requires a minimum of four sugar units in substrates
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
enzyme shows high endo-beta-1,4-mannanase activity versus various mannans, but low endo-beta-1,4 glucanase activity towards carboxymethylcellulose, andd negligible activity towards glucomannans
-
-
?
additional information
?
-
-
enzyme shows high endo-beta-1,4-mannanase activity versus various mannans, but low endo-beta-1,4 glucanase activity towards carboxymethylcellulose, andd negligible activity towards glucomannans
-
-
?
additional information
?
-
enzyme shows high endo-beta-1,4-mannanase activity versus various mannans, but low endo-beta-1,4 glucanase activity towards carboxymethylcellulose, andd negligible activity towards glucomannans
-
-
?
additional information
?
-
no activity with mannotriose, mannobiose, starch, carboxy methylcellulose, and birchwood xylan
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
enzyme is active in hydrolyzing the beta-mannan-rich cell wall of soybean seeds
-
-
?
additional information
?
-
-
enzyme degrades either beta-1,4-mannan or beta-1,4-mannooligosaccharides to mannotriose and mannotetraose. Enzyme disperses the fronds of the red alga Porphyra yezoensis into cell masses consisting of 10-20 cells that are available for cell engineering
-
-
?
additional information
?
-
during hydrolysis of 1,4-beta-manno-oligosaccharides, transglycosylation reactions occur
-
-
?
additional information
?
-
-
during hydrolysis of 1,4-beta-manno-oligosaccharides, transglycosylation reactions occur
-
-
?
additional information
?
-
-
the enzyme hydrolyzes high-molecular weight polysaccharides with beta-1,4-glycosidic bonds
-
-
?
additional information
?
-
-
main by products of the hydrolysis of both guar and locust bean gum are mannose and manno-oligosaccharides of different sizes (mannobiose, mannotriose and mannotetraose). Enzyme mode of action involving a transglycosylation reaction in the mechanism that allows the enzyme to hydrolyze this manno-oligosaccharide. No activity with mannobiose and mannotriose
-
-
?
additional information
?
-
no activity with 4-nitrophenyl beta-D-mannopyranoside
-
-
?
additional information
?
-
-
no activity with carboxymethyl cellulose
-
-
?
additional information
?
-
-
no activity with carboxymethyl cellulose
-
-
?
additional information
?
-
-
no substrate: xylan, caroxymethyl cellulose, cellulose, mannan
-
-
?
additional information
?
-
the native wild-type enzyme shows bifunctional activity as both an endo-glucanase and an endo-mannanase, substrate specificity, overview
-
-
?
additional information
?
-
-
the native wild-type enzyme shows bifunctional activity as both an endo-glucanase and an endo-mannanase, substrate specificity, overview
-
-
?
additional information
?
-
the enzyme also show transglycosylation activity
-
-
?
additional information
?
-
-
the enzyme also show transglycosylation activity
-
-
?
additional information
?
-
the native wild-type enzyme shows bifunctional activity as both an endo-glucanase and an endo-mannanase, substrate specificity, overview
-
-
?
additional information
?
-
the enzyme also show transglycosylation activity
-
-
?
additional information
?
-
no substrate: soluble starch, methylcellulose
-
-
?
additional information
?
-
-
no substrate: soluble starch, methylcellulose
-
-
?
additional information
?
-
no substrate: soluble starch, methylcellulose
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no activity with carboxymethyl cellulose, soluble starch, birchwood xylan, and pectin
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the enzyme catalyzes the random hydrolysis of beta-1,4-mannosidic linkages in the main chain of mannans, glucomannans and galactomannans, main products are mannobiose, mannotriose, and mannopentaose
-
-
?
additional information
?
-
-
the enzyme catalyzes the random hydrolysis of beta-1,4-mannosidic linkages in the main chain of mannans, glucomannans and galactomannans, main products are mannobiose, mannotriose, and mannopentaose
-
-
?
additional information
?
-
-
no substrate: carboxymethyl cellulose, oat spelt xylan, starch, pectin, 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
additional information
?
-
-
no substrate: carboxymethyl cellulose, oat spelt xylan, starch, pectin, 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
additional information
?
-
Penicillium wortmanni
-
-
-
-
?
additional information
?
-
enzyme exhibits substantial transglycosylase activity
-
-
?
additional information
?
-
-
no activity with tamarind xyloglucan, sodium arginate, carboxymethylcellulose, low-melting point agarose, gellan gum, xylan, carrageenan, and laminaran
-
-
?
additional information
?
-
-
the enzyme shows requirement of four mannose residues for hydrolysis, and is also capable of catalyzing transglycosylation reactions
-
-
?
additional information
?
-
requires at least five sugar moieties for effective catalytic activity, no substrate: yeast mannan
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
no activity against barley beta-glucan, birchwood xylan, and low viscosity carboxymethyl cellulose
-
-
?
additional information
?
-
-
no activity against barley beta-glucan, birchwood xylan, and low viscosity carboxymethyl cellulose
-
-
?
additional information
?
-
the enzyme catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides, such as glucomannans and galactomannans. Protein-ligand interactions from crystal structure analysis, circular dichroism spectroscopy, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides, such as glucomannans and galactomannans. Protein-ligand interactions from crystal structure analysis, circular dichroism spectroscopy, overview
-
-
?
additional information
?
-
the enzyme catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides, such as glucomannans and galactomannans. Protein-ligand interactions from crystal structure analysis, circular dichroism spectroscopy, overview
-
-
?
additional information
?
-
the wild-type enzyme can perform transglycosylation on to saccharide acceptors while the R171K mutant cannot Wild-type and mutant enzyme show the ability to perform alcoholysis reactions with methanol and butanol, forming new beta-linked glycoconjugates. It appears that the wild-type enzyme produces mainly mannobiose conjugates using mannotetetraoses substrate, while in contrast the R171K mutant produces mainly mannotriose conjugates, due to the altered subsite binding
-
-
?
additional information
?
-
-
transglycosylation reaction, Streptomyces: transfer of one mannose unit from oligosaccharides, fenugreek: transfer of oligomannose residues
-
-
?
additional information
?
-
-
transglycosylation reaction, Streptomyces: transfer of one mannose unit from oligosaccharides, fenugreek: transfer of oligomannose residues
-
-
?
additional information
?
-
enzyme has the ability to bind soluble beta-mannans
-
-
?
additional information
?
-
-
enzyme has the ability to bind soluble beta-mannans
-
-
?
additional information
?
-
enzyme hydrolyzes homopolysaccharides such as codium mannan, Porphyra mannan, coffee mannan, and coconut mannan, to form mainly mannobiose and mannotriose in addition to minor sugars, such as mannose, mannotetraose, and mannopentaose
-
-
?
additional information
?
-
-
enzyme hydrolyzes homopolysaccharides such as codium mannan, Porphyra mannan, coffee mannan, and coconut mannan, to form mainly mannobiose and mannotriose in addition to minor sugars, such as mannose, mannotetraose, and mannopentaose
-
-
?
additional information
?
-
enzyme has the ability to bind soluble beta-mannans
-
-
?
additional information
?
-
enzyme hydrolyzes homopolysaccharides such as codium mannan, Porphyra mannan, coffee mannan, and coconut mannan, to form mainly mannobiose and mannotriose in addition to minor sugars, such as mannose, mannotetraose, and mannopentaose
-
-
?
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2-mercaptoethanol
1 mM, 54% residual activity
4-nitrophenyl-thio-beta-D-mannopyranoside
-
-
abscisic acid
-
presence of exogenous abscisic acid provokes a delay in the cellular disassembly of the endosperm and disappearance of endo-beta-mannanase in the tissue, resulting in delayed galactomannan degradation
acetonitrile
about 55% residual activity at 10% (w/v)
Benzene
complete inhibition at 10% (w/v)
chloroform
complete inhibition at 10% (w/v)
CTAB
complete inhibition at 10% (v/v)
Cyclohexane
about 5% residual activity at 10% (w/v)
guanidine hydrochloride
-
20.5% residual activity at 1 mM
Isopropanol
-
about 60% residual activity at 20% (v/v)
n-Heptanol
about 5% residual activity at 10% (w/v)
n-hexane
about 5% residual activity at 10% (w/v)
n-Hexanol
about 5% residual activity at 10% (w/v)
n-Pentanol
about 10% residual activity at 10% (w/v)
Na+
87% residual activity at 1 mM
p-chloromercuribenzoate
-
-
phenylmethylsulfonyl fluoride
-
80.3% residual activity at 5 mM
Toluene
about 5% residual activity at 10% (w/v)
TritonX-100
-
about 40% residual activity at 10% (v/v)
Tween 40
about 58% residual activity at 10% (v/v)
Tween 80
about 61% residual activity at 10% (v/v)
Tween-20
-
about 50% residual activity at 10% (v/v)
Urea
about 70% residual activity at 100 mM
Ag+
-
-
Ag+
strong inhibition at 1 mM
Ag+
-
complete inhibition at 1 mM
Ag+
-
48% residual activity
Ag+
-
complete inhibition
Ag+
96% residual activity at 1 mM
Ag+
-
1 mM, 54% residual activity
Ag+
-
1 mM, 3% residual activity
Ag+
-
35.7% residual activity at 5 mM
Ag+
5 mM, 24.8% residual activity
Ag+
1 mM, 12% residual activity
Ag+
-
1 mM, complete loss of activity
Ag+
1 mM, 2% residual activity
Ag+
5 mM, complete loss of activity
Ag+
1 mM, more than 80% inhibition
Ag+
1 mM, 18% residual activity
Al3+
-
Al3+
-
84.7% residual activity at 5 mM
Al3+
1 mM, more than 80% inhibition
Al3+
1 mM, 31% residual activity
Ca2+
1 mM, 83% residual activity
Ca2+
-
2 mM, 64% residual activity. Stimulating above 2.5 mM
Ca2+
-
34.36% residual activity at 5 mM
Co2+
-
32% residual activity at 1 mM
Co2+
-
1 mM, 50% loss of activity
Co2+
about 90% residual activity at 1 mM
Co2+
-
2.5 mM, 42% residual activity
Cr3+
-
-
Cu2+
-
-
Cu2+
strong inhibition at 1 mM
Cu2+
-
75.1% residual activity at 1 mM
Cu2+
-
complete inhibition
Cu2+
-
72% inhibition at 20 mM
Cu2+
-
95.2% residual activity at 5 mM
Cu2+
more than 50% inhibition
Cu2+
1 mM, 8% residual activity
Cu2+
-
1 mM, 49% loss of activity
Cu2+
1 mM, 12% residual activity
Cu2+
1 mM, 76% residual activity
Cu2+
-
28% inhibition at 5 mM
Cu2+
1 mM, more than 80% inhibition
Cu2+
1 mM, 2% residual activity
dithiothreitol
-
85.5% residual activity at 5 mM
dithiothreitol
-
1 mM, 25% loss of activity
EDTA
-
-
EDTA
-
1 mM, 33.9% residual activity
EDTA
78% residual activity at 1 mM
EDTA
-
1 mM, 37% residual activity
EDTA
-
26.8% residual activity at 5 mM
EDTA
5 mM, 20% residaul activity
EDTA
-
28% inhibition at 5 mM
EDTA
-
2.5 mM, 77% residual activity
ethanol
-
about 60% residual activity at 20% (v/v)
Fe2+
-
1.5% residual activity at 1 mM
Fe2+
-
38% inhibition at 20 mM
Fe2+
more than 50% inhibition
Fe2+
-
1 mM, 40% loss of activity
Fe2+
about 35% residual activity at 1 mM
Fe3+
-
-
Fe3+
-
complete inhibition at 1 mM
Fe3+
-
30.6% residual activity
Fe3+
-
80.9% residual activity at 1 mM
Fe3+
1 mM, 42% residual activity
Fe3+
-
2.5 mM, 71% residual activity
Fe3+
1 mM, 37% residual activity
Hg2+
-
-
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
complete inhibition
Hg2+
4% residual activity at 1 mM
Hg2+
-
1 mM, 2% residual activity
Hg2+
5 mM, 16.4% residual activity
Hg2+
complete inhibition at 1 mM
Hg2+
1 mM, 8% residual activity
Hg2+
1 mM, 4% residual activity
Hg2+
-
complete inhibition at 1 mM
Hg2+
1 mM, more than 80% inhibition
Hg2+
1 mM, 1% residual activity
K+
-
-
K+
1 mM, 62% residual activity
Li+
-
-
Li+
-
96.3% residual activity at 1 mM
methanol
-
about 60% residual activity at 20% (v/v)
Mg2+
-
84% residual activity
Mg2+
-
1 mM, 53% residual activity
Mg2+
1 mM, 34% residual activity
Mg2+
-
89.7% residual activity at 5 mM
Mn2+
-
44.8% residual activity at 1 mM
Mn2+
35% of initial activity
Mn2+
67% residual activity at 1 mM
Mn2+
-
1 mM, 22% residual activity
Mn2+
-
89.6% residual activity at 5 mM
Mn2+
5 mM, 32% residual activity
Mn2+
-
5 mM, 50% residual activity
Mn2+
about 93% residual activity at 1 mM
Mn2+
1 mM, 63% residual activity
N-bromosuccinimide
-
complete inhibition
N-bromosuccinimide
-
1 mM, 3% residual activity
N-bromosuccinimide
-
complete inhibition at 5 mM
n-butanol
-
complete inhibition at 20-30% v/v
n-butanol
complete inhibition at 10% (w/v)
Ni2+
-
22.1% residual activity at 1 mM
Ni2+
-
1 mM, 61% residual activity
Pb2+
-
-
Pb2+
-
1.0% residual activity at 1 mM
Pb2+
1 mM, more than 80% inhibition
SDS
strong inhibition at 1 mM
SDS
-
about 45% residual activity at 10% (w/v)
SDS
-
complete inhibition at 0.25-1.0% w/v
SDS
-
79.7% residual activity at 5 mM
SDS
0.5%, 1% residual activity
SDS
complete inhibition at 10% (w/v)
SDS
-
the enzyme shows about 45% activity in the presence of 10% (w/v) SDS
Sodium dodecyl sulfate
20% of initial activity
Sodium dodecyl sulfate
strong
Sodium dodecyl sulfate
strong inhibition
sodium dodecylsulfate
-
1 mM, 55% residual activity
sodium dodecylsulfate
-
1 mM, 79% residual activity
Triton X-100
-
-
Triton X-100
0.5%, 44% residual activity
Triton X-100
about 55% residual activity at 10% (v/v)
Tween 20
-
-
Tween 20
0.5%, 77% residual activity
Tween 20
about 60% residual activity at 10% (v/v)
Zn2+
-
-
Zn2+
-
1.1% residual activity at 1 mM
Zn2+
-
68% residual activity
Zn2+
-
95% residual activity at 5 mM
Zn2+
more than 50% inhibition
Zn2+
-
90.9% residual activity at 5 mM
Zn2+
5 mM, partial loss of activity
Zn2+
1 mM, more than 80% inhibition
Zn2+
1 mM, 16% residual activity
additional information
-
the purified recombinant enzyme has a strong resistance to SDS and Ag+ and proteases pepsin and trypsin
-
additional information
-
not inhibitory: EDTA, phenyl methyl sulfonyl fluoride, 1,10-phenanthroline
-
additional information
-
EDTA does not affect the activity of the enzyme
-
additional information
-
not inhibitory: EDTA, 2-mercaptoethanol
-
additional information
enzymatic activity is not significantly affected by ions such as Ca2+, Cr3+, Co2+, Zn2+, Na+, K+, and Mg2+
-
additional information
not inhibitory: EDTA, dithiothreitol
-
additional information
-
not inhibitory: EDTA, dithiothreitol
-
additional information
EDTA has no effect on enzyme activity
-
additional information
not inhibitory: Mg2+, Co2+, EDTA
-
additional information
-
Ca2+, Mg2+, Mn2+, Fe2+, Ni2+, and Zn2+ have either no effect or a slightly inhibitory effect
-
additional information
-
not influenced by Triton X-100 and Tween-20 (10% (v/v)
-
additional information
presence of Ca2+, Na+, Mg2+, Mn2+, urea, and EDTA does not affect catalytic activity
-
additional information
-
presence of Ca2+, Na+, Mg2+, Mn2+, urea, and EDTA does not affect catalytic activity
-
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0.00066 - 0.04
2,4-dinitrophenyl-beta-mannobioside
0.25 - 0.46
4-methylumbelliferyl mannotrioside
0.592 - 1.3
locust bean gum
-
3.07 - 3.12
low viscosity locust bean galactomannan
-
1.6 - 2.9
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
0.6 - 1.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
9
Manbeta(1-4)Manbeta(1-4)Man
-
-
2.49
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
-
1.61 - 5.3
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
0.5
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
-
0.31 - 10.6
Mannotetraose
additional information
carob galactomannan
-
0.00066
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant E212A
0.00074
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant Y285A
0.0014
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant D283H
0.0037
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant H211A/D283A
0.0068
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant H211A
0.0093
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, wild type
0.01
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant H211N
0.0141
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant W162A
0.0149
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant W156A
0.0166
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant D283A
0.0205
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant W217A
0.04
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant H143A
0.25
4-methylumbelliferyl mannotrioside
pH 40°C, pH 4.5, wild-type enzyme
0.46
4-methylumbelliferyl mannotrioside
pH 40°C, pH 4.5, mutant enzyme R171K
0.592
locust bean gum
-
pH and temperature not specified in the publication
-
0.6
locust bean gum
pH 40°C, pH 4.5, wild-type enzyme
-
1.3
locust bean gum
pH 40°C, pH 4.5, mutant enzyme R171K
-
3.07
low viscosity locust bean galactomannan
-
isozyme MAN I
-
3.12
low viscosity locust bean galactomannan
-
isozyme MAN II
-
1.6
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
1.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
wild-type, pH 5.5, 37°C
2.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
2.9
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
pH 5.5, 37°C
0.6
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
wild-type, pH 5.5, 37°C
1
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
1.3
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
1.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
pH 5.5, 37°C
1.61
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
-
5.3
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
30°C, pH 4.8
0.05
mannohexaose
pH 40°C, pH 4.5, wild-type enzyme
0.34
mannohexaose
pH 40°C, pH 4.5, mutant enzyme R171K
0.08
Mannopentaose
pH 40°C, pH 4.5, wild-type enzyme
1.7
Mannopentaose
pH 40°C, pH 4.5, mutant enzyme R171K
0.31
Mannotetraose
pH 40°C, pH 4.5, wild-type enzyme
10.6
Mannotetraose
pH 40°C, pH 4.5, mutant enzyme R171K
additional information
carob galactomannan
Km value 2.22 mg/ml, pH 5.0, 60°C
-
additional information
carob galactomannan
-
Km value 2.22 mg/ml, pH 5.0, 60°C
-
additional information
konjac glucomannan
Km value 3.22 mg/ml, pH 5.0, 60°C
-
additional information
konjac glucomannan
-
Km value 3.22 mg/ml, pH 5.0, 60°C
-
additional information
konjac glucomannan
Km value 4.7 mg/ml, pH 5.4, 70°C
-
additional information
konjac glucomannan
-
Km value 4.7 mg/ml, pH 5.4, 70°C
-
additional information
locust bean gum
KM value is 3.8 mg/ml
-
additional information
locust bean gum
-
KM value is 34.9 mg/ml, pH 5.0, 28°C
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
copra beta-mannan: 2.0 mg/ml, locust bean beta-mannan: 3.8 mg/ml, konjak beta-mannan: 7.7 mg/ml, carob galactomannan: 0.9 mg/ml
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
apparent Km values of the mannanase for locust bean gum, glucomannan, glactomannan and mannan are 3, 2.3, 1.6 and 0.54 mg/ml, respectively
-
additional information
additional information
-
apparent Km values of the mannanase for locust bean gum, guar gum and konjac powder are 7.6, 10.5 and 27.4 mg/ml, respectively
-
additional information
additional information
Km value for locust bean gum at pH 2.4, 50°C is 0.93 mg/ml
-
additional information
additional information
-
Km value for locust bean gum at pH 2.4, 50°C is 0.93 mg/ml
-
additional information
additional information
Km value is 0.16 mg/ml for locust-bean galactomannan
-
additional information
additional information
-
Km value is 0.16 mg/ml for locust-bean galactomannan
-
additional information
additional information
-
Km value for konjac flour is 7.5 mg/ml, for locust bean gum 11.67 mg/ml
-
additional information
additional information
Km value for konjac glucomannan 0.6 mg/ml
-
additional information
additional information
-
Km value for konjac glucomannan 0.6 mg/ml
-
additional information
additional information
Km values are 14.9 mg/ml, 17.5 mg/ml, and 15.2 mg/ml for glucomannan, locust bean gum and beta-D-mannan, respectively
-
additional information
additional information
-
Km values are 14.9 mg/ml, 17.5 mg/ml, and 15.2 mg/ml for glucomannan, locust bean gum and beta-D-mannan, respectively
-
additional information
additional information
Km values for konjac glucomannan of low viscosity, locust bean gum galactomannan, carob galactomannan of low viscosity, and 1,4-beta-D-mannan from carob are 0.6 mg/ml, 2.0 mg/ml, 2.2 mg/ml and 1.5 mg/ml, respectively
-
additional information
additional information
-
Km values for konjac glucomannan of low viscosity, locust bean gum galactomannan, carob galactomannan of low viscosity, and 1,4-beta-D-mannan from carob are 0.6 mg/ml, 2.0 mg/ml, 2.2 mg/ml and 1.5 mg/ml, respectively
-
additional information
additional information
-
Km values for locust bean gum, guar gum, and copra mannan, are 0.11, 0.28, and 0.33 mg/ml, respectively
-
additional information
additional information
kinetics of recombinant chimeric enzymes, overview
-
additional information
additional information
-
Km is 2.074 mg/ml with guar gum for the recombinant enzyme at pH 5.5 and 30°C
-
additional information
additional information
Km of the recombinant enzyme is 7.8 mg/ml for locust bean gum, pH 4.5, 50°C
-
additional information
additional information
-
Km values of the recombinant enzyme are 3.78 mg/ml for locust bean gum, and 7.75 mg/ml for guar gum
-
additional information
additional information
-
Km values with ocust bean gum are 0.9 mg/ml for wild-type enzyme, 0.8 mg/ml for mutant Man5DELTACBM, and 1.1 mg/ml for mutant Man5DELTACL
-
additional information
additional information
-
Michaelis-Menten kinetics, Km values for locust bean gum, konjac mannan, and guar gum are 7.6 mg/ml, 2.1 mg/ml, and 2.3 mg/ml, respectively, pH 4.0, 80°C
-
additional information
additional information
-
recombinant enzyme, Km for locust bean gum is 0.83 ± 0.2 mg/ml, pH 4.0, 80°C
-
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evolution
the enzyme belongs to the glycosyl hydrolae famiyl 5, GH5
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
evolution
the enzyme belongs to the glycosyl hydrolase family 5, GH5
evolution
the enzyme belongs to the glycosyl hydrolase family 5, GH5
evolution
the enzyme belongs to the glycosyl hydrolase family 5, GH5, structure comparisons, the overall fold of the enzyme is strongly conserved, overview. The enzyme displays the typical (beta/alpha)8-barrel fold and a unique structural arrangement of three surface loops that stretch over the active centre, promoting an altered topography of the binding cleft
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5, structure comparisons, the overall fold of the enzyme is strongly conserved, overview. The enzyme displays the typical (beta/alpha)8-barrel fold and a unique structural arrangement of three surface loops that stretch over the active centre, promoting an altered topography of the binding cleft
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
-
metabolism
key enzyme for hydrolyzing mannan, a major constituent of hemicellulose
metabolism
the enzyme is involved in the hydrolysis of plant cell wall mannans and heteromannans
metabolism
-
key enzyme for hydrolyzing mannan, a major constituent of hemicellulose
-
physiological function
when endo-beta-mannanase activity is much reduced by RNAi and antisense RNA strategies, their firmness is higher compared to those of control fruits at the turning and orange-color stages, but at the red-ripe stage firmness is similar between the two fruit-types
physiological function
enzyme strongly binds to ivory nut mannan, Avicel, chitosan, and chitin, but does not attach to curdlan, insoluble oat spelt xylan, lignin, or poly(3-hydroxybutyrate)
physiological function
germination time in T-DNA insertion mutant almost doubles compared to wild-type. Enzyme is important for the germination of Arabidopsis thaliana seeds by facilitating the hydrolysis of the mannan-rich endosperm cell walls
physiological function
T-DNA insertion mutant germinates later than the wild type. Enzyme is important for the germination of Arabidopsis thaliana seeds by facilitating the hydrolysis of the mannan-rich endosperm cell walls
physiological function
the enzyme beta-mannanase is responsible for the cleavage of beta-1,4-linked internal linkages of the mannan polymer to produce new chain ends
physiological function
-
strain is not an effective producer of mannan-degrading enzymes. Oat spelt xylan is the best inducer of mannanase, feruloyl esterase, arabinofuranosidase, glucosidase and acetyl xylan esterase
physiological function
-
enzyme strongly binds to ivory nut mannan, Avicel, chitosan, and chitin, but does not attach to curdlan, insoluble oat spelt xylan, lignin, or poly(3-hydroxybutyrate)
-
physiological function
-
strain is not an effective producer of mannan-degrading enzymes. Oat spelt xylan is the best inducer of mannanase, feruloyl esterase, arabinofuranosidase, glucosidase and acetyl xylan esterase
-
physiological function
-
the enzyme beta-mannanase is responsible for the cleavage of beta-1,4-linked internal linkages of the mannan polymer to produce new chain ends
-
additional information
-
catalytic residues are Glu181 as catalytic acid/base and Glu288 as nucleophile, molecular docking study with different manno-configured ligands from mannobiose to mannohexose as well as galactomannan. The ability to accommodate larger ligand molecules in the active site of CtManT is probably due to the long loops enclosing the active site that provides the depth of the cavity, structure overview
additional information
tertiary structure, active site and substrate binding site structures analysis, detailed overview. Two tryptophan residues that provide the hydrophobic stacking of the +1 subsite Trp125 and Trp271,is 9.5 A, making bulkier branched substrates difficult to accommodate
additional information
-
tertiary structure, active site and substrate binding site structures analysis, detailed overview. Two tryptophan residues that provide the hydrophobic stacking of the +1 subsite Trp125 and Trp271,is 9.5 A, making bulkier branched substrates difficult to accommodate
additional information
the enzyme has an extended loop that alters topography of the active site, structural and mutational analyses, overview. The extended loop is linked to the cold-adapted enzymatic activity, structure of mannose-recognition subsites. Glu181 and Glu312 are highly conserved catalytic residues, Glu181 is the catalytic acid/base, and Glu312 is the nucleophile. Trp341, which is located in the vicinity of the catalytic residues, acts as a hydrophobic platform for sugar binding in catalytic site, the enzyme also has a second mannan binding site. Sequence comparisons, overview
additional information
-
the enzyme has an extended loop that alters topography of the active site, structural and mutational analyses, overview. The extended loop is linked to the cold-adapted enzymatic activity, structure of mannose-recognition subsites. Glu181 and Glu312 are highly conserved catalytic residues, Glu181 is the catalytic acid/base, and Glu312 is the nucleophile. Trp341, which is located in the vicinity of the catalytic residues, acts as a hydrophobic platform for sugar binding in catalytic site, the enzyme also has a second mannan binding site. Sequence comparisons, overview
additional information
the enzyme is composed of three distinct domains and shows some level of molecular flexibility in solution, nevertheless it has a preferred conformation, which can be described by the rigid-body modeling procedure, structure analysis. The enzyme contains a linker with a compact structure that occupies a small volume with respect to its large number of amino acids, role of the length and flexibility of the linker on the spatial arrangement of the constitutive domains. The linker can optimize the geometry between the other two domains with respect to the substrate at high temperatures. The hydrodynamic radii of full-length enzyme and single catalytic domain are independent of protein concentration over the range 0.5 to 8 mg/ml at 20°C and pH 6
additional information
-
the enzyme is composed of three distinct domains and shows some level of molecular flexibility in solution, nevertheless it has a preferred conformation, which can be described by the rigid-body modeling procedure, structure analysis. The enzyme contains a linker with a compact structure that occupies a small volume with respect to its large number of amino acids, role of the length and flexibility of the linker on the spatial arrangement of the constitutive domains. The linker can optimize the geometry between the other two domains with respect to the substrate at high temperatures. The hydrodynamic radii of full-length enzyme and single catalytic domain are independent of protein concentration over the range 0.5 to 8 mg/ml at 20°C and pH 6
additional information
the structure of the catalytic domain reveals a canonical (alpha/beta)8-barrel scaffold surrounded by loops and short helices that form the catalytic interface, subsites forming the active-site cleft with residues W134, E198, R200, E235, H283 and W284 are directly involved in glucose binding, structure analysis of full-length enzyme and catalytic domain, overview
additional information
-
the structure of the catalytic domain reveals a canonical (alpha/beta)8-barrel scaffold surrounded by loops and short helices that form the catalytic interface, subsites forming the active-site cleft with residues W134, E198, R200, E235, H283 and W284 are directly involved in glucose binding, structure analysis of full-length enzyme and catalytic domain, overview
additional information
-
tertiary structure, active site and substrate binding site structures analysis, detailed overview. Two tryptophan residues that provide the hydrophobic stacking of the +1 subsite Trp125 and Trp271,is 9.5 A, making bulkier branched substrates difficult to accommodate
-
additional information
-
catalytic residues are Glu181 as catalytic acid/base and Glu288 as nucleophile, molecular docking study with different manno-configured ligands from mannobiose to mannohexose as well as galactomannan. The ability to accommodate larger ligand molecules in the active site of CtManT is probably due to the long loops enclosing the active site that provides the depth of the cavity, structure overview
-
additional information
-
the structure of the catalytic domain reveals a canonical (alpha/beta)8-barrel scaffold surrounded by loops and short helices that form the catalytic interface, subsites forming the active-site cleft with residues W134, E198, R200, E235, H283 and W284 are directly involved in glucose binding, structure analysis of full-length enzyme and catalytic domain, overview
-
additional information
-
the enzyme is composed of three distinct domains and shows some level of molecular flexibility in solution, nevertheless it has a preferred conformation, which can be described by the rigid-body modeling procedure, structure analysis. The enzyme contains a linker with a compact structure that occupies a small volume with respect to its large number of amino acids, role of the length and flexibility of the linker on the spatial arrangement of the constitutive domains. The linker can optimize the geometry between the other two domains with respect to the substrate at high temperatures. The hydrodynamic radii of full-length enzyme and single catalytic domain are independent of protein concentration over the range 0.5 to 8 mg/ml at 20°C and pH 6
-
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113000
x * 113000, deduced from gene sequence, upon expression in Escherichia coli, two fragments of 45000 and 50000 Da
145294
-
x * 145294, calculated
162000
-
dimeric protein, SDS-PAGE
26000
-
x * 26000, SDS-PAGE
31000
x * 31000, SDS-PAGE
32000
x * 32000, calculated and SDS-PAGE
35500
-
x * 35500, recombinant His6-tagged enzyme, SDS-PAGE, x * 33000, about, enzyme without signal sequence, sequence calculation
37700
-
x * 37700, calculated
38013
-
x * 38013, calculated, x * 38000, SDS-PAGE, mature protein
38950
calculation from sequence of DNA
39216
-
1 * 39216, ManA, 1 * 39265, ManB, MALDI-TOF spectrometry
39265
-
1 * 39216, ManA, 1 * 39265, ManB, MALDI-TOF spectrometry
39500
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE
39600
-
x * 39600, SDS-PAGE
39627
-
x * 39000, SDS-PAGE, x * 39627, calculated for mature protein
39961
x * 39961, calculated
41389
x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
42400
x * 42400, deduced from gene sequence, mature protein
43100
-
calculation from sequence of DNA
43767
x * 44000, SDS-PAGE, x * 43767, calculated
43847
x * 56000, SDS-PAGE, x * 43847, calculated
44300
-
x * 44300, SDS-PAGE
46644
x * 56000, SDS-PAGE, x * 46644, calculated
46800
x * 46800, SDS-PAGE
48000
x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
53600
x * 53600, calculated
66000
-
1 * 66000, SDS-PAGE
72000
x * 72000, recombinant enzyme, SDS-PAGE, x * 43000, about, sequence calculation of the mature enzyme
73588
1 * 76309, calculated including signal peptide, 1 * 73588, calculated, mature protein, 1 * 73000, SDS-PAGE
76309
1 * 76309, calculated including signal peptide, 1 * 73588, calculated, mature protein, 1 * 73000, SDS-PAGE
33000
Lilium testaceum
-
gel filtration
33000
x * 33000, SDS-PAGE and calculated
33000
-
x * 35500, recombinant His6-tagged enzyme, SDS-PAGE, x * 33000, about, enzyme without signal sequence, sequence calculation
37000
-
SDS-PAGE
38000
-
gel filtration
38000
-
x * 38000, SDS-PAGE
38000
-
x * 38013, calculated, x * 38000, SDS-PAGE, mature protein
38000
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
39000
-
SDS-PAGE
39000
-
SDS-PAGE, 40000 by gel filtration
39000
method not mentioned
39000
-
gel filtration, ManA and ManB
39000
-
x * 39000, SDS-PAGE, x * 39627, calculated for mature protein
39000
x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
40000
-
-
40000
-
x * 40000, SDS-PAGE
40000
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE
41000
-
SDS-PAGE
41000
-
recombinant protein expressed in E. coli, SDS-PAGE
41000
x * 45000, SDS-PAGE, x * 41000, calculated
41000
-
x * 41000, recombinant enzyme, SDS-PAGE
41000
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
43000
gel filtration
43000
x * 43000, SDS-PAGE
43000
-
x * 43000, recombinant enzyme, SDS-PAGE
43000
-
x * 43000, ManB, SDS-PAGE
43000
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE
43000
x * 72000, recombinant enzyme, SDS-PAGE, x * 43000, about, sequence calculation of the mature enzyme
44000
-
SDS-PAGE
44000
x * 44000, SDS-PAGE
44000
x * 44000, SDS-PAGE, x * 43767, calculated
45000
-
-
45000
-
recombinant protein expressed in Aspergillus oryzae, SDS-PAGE
45000
x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
45000
x * 45000, SDS-PAGE, x * 41000, calculated
50000
-
SDS-PAGE, a stable fragment corresponding to about 460 residues and comprising the catalytic domain and 50 to 60 extra residues at the C-terminus
50000
x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
53000
-
SDS-PAGE
53000
x * 53000, SDS-PAGE
55000
-
-
55000
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
56000
x * 56000, SDS-PAGE, x * 43847, calculated
56000
x * 56000, SDS-PAGE, x * 46644, calculated
58000
-
M-I, SDS-PAGE
58000
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
60000
-
isozyme MAN I, SDS-PAGE
60000
x * 60000, SDS-PAGE, recombinant enzyme
60000
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
63000
-
isozyme MAN II, SDS-PAGE
63000
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
65000
-
PAGE
65000
x * 65000, SDS-PAGE
70000
-
gel filtration
70000
-
x * 70000, SDS-PAGE, recombinant protein including His-tag
73000
-
2 * 73000, SDS-PAGE
73000
1 * 76309, calculated including signal peptide, 1 * 73588, calculated, mature protein, 1 * 73000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
-
2 * 73000, SDS-PAGE
?
-
x * 38000, SDS-PAGE
?
-
x * 38000, SDS-PAGE
-
?
x * 39200, calculated from amino acid sequence
?
-
x * 34300, calculated from amino acid sequence
?
-
x * 34000, SDS-PAGE
-
?
-
x * 34300, calculated from amino acid sequence
-
?
x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
?
-
x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
-
?
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE
?
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE
-
?
x * 60000, SDS-PAGE, recombinant enzyme
?
-
x * 60000, SDS-PAGE
-
?
x * 56000, SDS-PAGE, x * 43847, calculated
?
x * 56000, SDS-PAGE, x * 46644, calculated
?
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
?
-
x * 56000, SDS-PAGE, x * 43847, calculated
-
?
-
x * 56000, SDS-PAGE, x * 46644, calculated
-
?
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
-
?
-
x * 37700, calculated
?
-
x * 53000, SDS-PAGE
-
?
-
x * 37700, calculated
-
?
-
x * 45000, SDS-PAGE
-
?
x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
?
x * 45000, SDS-PAGE, x * 41000, calculated
?
x * 38000, native purified enzyme, SDS-PAGE
?
x * 54000, recombinant protein, SDS-PAGE
?
-
x * 38013, calculated, x * 38000, SDS-PAGE, mature protein
?
-
x * 41000, recombinant enzyme, SDS-PAGE
?
-
x * 38013, calculated, x * 38000, SDS-PAGE, mature protein
-
?
-
x * 41000, recombinant enzyme, SDS-PAGE
-
?
-
x * 39600, SDS-PAGE
-
?
-
x * 40000, SDS-PAGE
-
?
x * 44000, SDS-PAGE, x * 43767, calculated
?
-
x * 44000, SDS-PAGE, x * 43767, calculated
-
?
-
x * 70000, SDS-PAGE, recombinant protein including His-tag
?
-
x * 43000, ManB, SDS-PAGE
?
-
x * 39000, SDS-PAGE, x * 39627, calculated for mature protein
?
-
x * 35500, recombinant His6-tagged enzyme, SDS-PAGE, x * 33000, about, enzyme without signal sequence, sequence calculation
?
-
x * 43000, SDS-PAGE
-
?
x * 32000, calculated and SDS-PAGE
?
-
x * 31000, SDS-PAGE
-
?
-
x * 32000, calculated and SDS-PAGE
-
?
-
x * 145294, calculated
?
-
x * 145294, calculated
-
?
-
x * 53600, calculated
-
?
x * 72000, recombinant enzyme, SDS-PAGE, x * 43000, about, sequence calculation of the mature enzyme
?
-
x * 72000, recombinant enzyme, SDS-PAGE, x * 43000, about, sequence calculation of the mature enzyme
-
?
-
x * 43000, recombinant enzyme, SDS-PAGE
?
x * 113000, deduced from gene sequence, upon expression in Escherichia coli, two fragments of 45000 and 50000 Da
?
x * 42400, deduced from gene sequence, mature protein
?
x * 60000, SDS-PAGE of recombinant protein, x * 50605, calculated
?
-
x * 44000, SDS-PAGE
-
?
x * 65000-70000, His6-tagged enzyme, SDS-PAGE
?
-
x * 65000-70000, His6-tagged enzyme, SDS-PAGE
-
?
x * 33000, SDS-PAGE and calculated
monomer
-
1 * 66000, SDS-PAGE
monomer
1 * 40000, SDS-PAGE, 1 * 40457, calculated
monomer
-
1 * 40000, SDS-PAGE, 1 * 40457, calculated
-
monomer
-
1 * 39216, ManA, 1 * 39265, ManB, MALDI-TOF spectrometry
monomer
1 * 50000, SDS-PAGE
monomer
-
1 * 50000, SDS-PAGE
-
monomer
-
1 * 38000, SDS-PAGE
monomer
-
1 * 38000, SDS-PAGE
-
monomer
1 * 76309, calculated including signal peptide, 1 * 73588, calculated, mature protein, 1 * 73000, SDS-PAGE
monomer
-
1 * 76309, calculated including signal peptide, 1 * 73588, calculated, mature protein, 1 * 73000, SDS-PAGE
-
monomer
-
1 * 36250, SDS-PAGE
monomer
-
1 * 36450, calculated from amino acid sequence
monomer
-
1 * 36250, SDS-PAGE
-
monomer
-
1 * 36450, calculated from amino acid sequence
-
additional information
-
the three-dimensional enzyme structure contains a (beta/alpha)8 TIM barrel folding motif
additional information
-
the three-dimensional enzyme structure contains a (beta/alpha)8 TIM barrel folding motif
-
additional information
-
the multimodular enzyme consists of a family 1 carbohydrate-binding module (CBM1), a Thr/Ser-rich linker region, and a catalytic domain
additional information
-
the multimodular enzyme consists of a family 1 carbohydrate-binding module (CBM1), a Thr/Ser-rich linker region, and a catalytic domain
-
additional information
-
Trp360 is critical in substrate binding at -1 subsite, Tyr285 works as nucleophile catalyst, Trp217 and Trp162 are important for the activity against mannooligosaccharides but less important for activity against polysaccharides
additional information
the enzyme adopts a TIM (beta/alpha)8-barrel fold
additional information
-
the enzyme adopts a TIM (beta/alpha)8-barrel fold
additional information
the enzyme adopts the (beta/alpha)8-barrel fold
additional information
-
the enzyme adopts the (beta/alpha)8-barrel fold
additional information
-
the enzyme adopts the (beta/alpha)8-barrel fold
-
additional information
C-terminal domain of 550 amino acid residues with homology to glycosidase family 26
additional information
the enzyme shows some level of molecular flexibility in solution and is composed of three distinct domains, a GH5 catalytic domain (373 amino acid residues) and a carbohydrate-binding domain (172 amino acid residues) connected through a linker (102 amino acid residues). Secondary structure, overview
additional information
-
the enzyme shows some level of molecular flexibility in solution and is composed of three distinct domains, a GH5 catalytic domain (373 amino acid residues) and a carbohydrate-binding domain (172 amino acid residues) connected through a linker (102 amino acid residues). Secondary structure, overview
additional information
the two-domain enzyme encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, structure analysis and comparisons, overview
additional information
-
the two-domain enzyme encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, structure analysis and comparisons, overview
additional information
-
the two-domain enzyme encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, structure analysis and comparisons, overview
-
additional information
-
the enzyme shows some level of molecular flexibility in solution and is composed of three distinct domains, a GH5 catalytic domain (373 amino acid residues) and a carbohydrate-binding domain (172 amino acid residues) connected through a linker (102 amino acid residues). Secondary structure, overview
-
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10 - 50
the enzyme retains 100% activity after 30 min at 10-50°C, at 60°C the activity drops to about 50%
10 - 80
varying residual activities of recombinant chimeric enzymes, overview
100
-
the enzyme shows 30% and 60% of the maximal activity after an incubation at 100°C for 120 min and 80°C for 60 min, respectively
20 - 50
-
purified enzyme, pH 8.0, 20 min, stable at
20 - 70
the enzyme shows good stability along 20-65°C and retains more than 60% of its activity for up to 1 h at 60°C. The enzyme has a half-life of 26xa0min at 70°C
30 - 60
the enzyme is stable up to 60°C for 1 h. At 70°C, the activity drops to less than 40% after 1h
30 - 90
-
purified recombinant wild-type enzyme, pH 5.0, 1 h, more than 45% of maximal activity at 50-80°C and over 30% activity at 90°C
35 - 45
-
the relatively high thermostability is retained after 1 h in the temperature range of 35-45°C and the stability rapidly decreases above 60°C
37 - 60
-
the enzyme shows 100%, 80%, 50%, 20% and no activity after 1 h at 37°C, 45°C, 50°C, 55°C, and 60°C, respectively
38
20 min, 50% residual activity, recombinant enzyme
39
-
4 h, stable between pH 5 and 7
40 - 70
more than 65% of maximum activity within
45 - 55
below 45°C, the recombinant enzyme remains stable with 95% glycosyl hydrolase activity for 1 h, but quickly loses this function above 55°C
50 - 85
the enzyme retains 60% activity at 80°C for 2 h and almost full enzyme activity remains after 4 h at 50°C. The enzyme retains 52 % enzyme activity at 85°C after 15 min
52
-
20 min, 50% residual activity
55.9
-
unfolding temperature
70 - 85
the free enzyme retains 42.5% residual activity after 35 min at 70-75°C. The half-lives of the free enzyme at 70, 75, 80 and 85°C are 138.6, 77, 24.7 and 25.6 min, respectively
70 - 90
-
after incubation at 70°C for 120 min, the enzyme activity toward glucomannan decreases to 50% of the maximal activity at 30°C. After incubation at 70°C for 120 min, the activity of the enzyme toward glucomannan decreases to 50% of the maximal activity at 30°C. The activity of the enzyme toward mannohexaose decreases to 73% after incubation at 70°C for 60 min. Further increases of temperature to 80 and 90°C for 60 min result in 70 and 26% of the enzyme activity remaining, respectively
75
-
30 min, 90% loss of activity
85
pH 6.0, the full-length enzyme is completely stable, while the isolated catalytic domain starts to precipitate
37
-
stable up to
37
purified reocmbinant enzyme, pH 4.5, 2 h, no loss of activity
40
-
stable up to
40
recombinant enzyme expressed in Aspergillus sojae
40
3 h, 95% residual activity
40 - 60
the enzyme maintains thermostability with 80% activity remaining at 40°C after 1 h and 60% activity remaining at 50°C after 1 h. When incubated at 60°C without substrate, the enzyme loses activity rapidly (about 25% residual activity after 10 min, no activity after 30 min)
40 - 60
-
the enzyme remains stable for 12 h at 40°C and exhibits about 30% activity after 2 h at 50°C. The enzyme shows no activity at 60°C
40 - 60
-
the enzyme is stable up to 60°C and retains 85% of its activity after 1.0 h of incubation
45
30 min, 60% rsidual activity
45
half-life less than 10 min
45
stable up to, for at least 20 min
50
recombinant enzyme expressed in Pichia pastoris
50
after incubation for 30 min, stable at pH 5-12. After incubation for 24 h, stable at pH 6-9. Half-life about 80 h at pH 6.0
50
-
pH 6-9, 1 h, 70% residual activity
50
pH 6.0, stable for 30 min, incubation without substrate
50
-
purified recombinant enzyme, pH 5.0-9.0, 8 h, stable at
50
-
30 min, 20% residual activity
50
60 min, 90% residual activity
50
retains 90% of its activity after incubation for 60 min
50
purified reocmbinant enzyme, pH 4.5, 90 min, loss of 50% activity
55
-
stable up to 55°C
55
-
6 h, 50% residual activity
55
-
purified recombinant enzyme, without substrate, stable up to, 90% activity remaning at 55°C after 30 min
55
-
15 min, almost complete loss of activity
60
-
5 h, more than 50% residual activity
60
-
a combination of mannanase with 0.2% sodium benzoate and 30% or 35% sorbitol presents the highest relative activity of about 150% when incubated at 60°C for 4 h, the control retains 63% of the initial activity
60
-
purified recombinant enzyme, 6 h, over 80% activity remaining
60
-
6 h, 50% residual activity
60
-
8 h, 50% residual activity
60
30 min, complete loss of activity
60
-
60 min, 90% residual activity
60
-
at pH 6.0, stable up to
60
20 min, complete loss of activity
60
but no activity remains after incubation for 20 min
60
the enzyme is completely stable at 60°C for 3 h
60
-
rapidly inactivated at 60°C
60
purified reocmbinant enzyme, pH 4.5, 30 min, complete loss of activity
60
-
purified recombinant His6-tagged enzyme, half-life is approximately 58 h at pH 4.0
60
-
30 min, stable up to
65
-
stable below
65
-
completely stable at
70
-
the enzyme exhibits god thermal stability at temperatures up to 70°C
70
-
recombinant protein from Aspergillus oryzae
70
-
purified recombinant enzyme, 80% activity remaining after 1 h, inactivation after 2 h
70
half-life 56 h, pH 4.0
70
-
30 min, 20% residual activity
70
20 min, 50% residual activity
70
2 h, 50% residual activtiy
70
-
purified enzyme, pH 8.0, 20 min, loss of 50% activity
70
1 h, 70% residual activity, truncated protein fragments produced in Escherichia coli, 1 h, 87% residual activity, protein derived from Rhodothermus marinus
80
-
2 min, complete loss of activity
80
-
20 min, 18% residual activity, 30 min, complete loss of activity
80
-
no loss of activity over 16 h
90
-
half-life 15 min
90
-
purified enzyme, pH 8.0, 20 min, inactivation
90
1 h, 25% residual activity, truncated protein fragments produced in Escherichia coli
additional information
-
glycerol at 30-40%, potassium sorbate/sodium benzoate at 0.2%, and sorbitol at 30-35% enhances enzyme thermostability and activity, overview
additional information
-
the glycosylation status of the enzyme has no effect on the thermostability
additional information
-
removal of the family 1 carbohydrate-binding module alone improves the thermostability of the enzyme, but additional removal of the linker region results in worse thermostability
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
the CBM27 accessory domain is critical for thermal stability, it reduces the melting temperature from 100°C to 88°C
additional information
-
the CBM27 accessory domain is critical for thermal stability, it reduces the melting temperature from 100°C to 88°C
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