Information on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.2.1.78
-
RECOMMENDED NAME
GeneOntology No.
mannan endo-1,4-beta-mannosidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Fructose and mannose metabolism
-
-
mannan degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
4-beta-D-mannan mannanohydrolase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1,4-beta-D-mannan mannanohydrolase
-
-
-
-
beta-1,4-mannan 4-mannanohydrolase
-
-
-
-
beta-D-mannanase
-
-
-
-
Beta-mannanase
-
-
-
-
beta-mannanase B
-
-
-
-
endo-1,4-beta-mannanase
-
-
-
-
Endo-1,4-mannanase
-
-
-
-
endo-beta-1,4-mannase
-
-
-
-
endo-beta-mannanase
-
-
-
-
mannanase, endo-1,4-beta-
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37288-54-3
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
anearogenes
-
-
Manually annotated by BRENDA team
Alicyclobacillus acidocaldarius Tc-12-31
strain Tc-12-31
-
-
Manually annotated by BRENDA team
member of glycosyl hydrolase family 5
-
-
Manually annotated by BRENDA team
MRC 11624
Uniprot
Manually annotated by BRENDA team
strain MRC11624
-
-
Manually annotated by BRENDA team
Aspergillus aculeatus MRC 11624
MRC 11624
Uniprot
Manually annotated by BRENDA team
Aspergillus aculeatus MRC11624
strain MRC11624
-
-
Manually annotated by BRENDA team
strain IMI 385708, formerly Thermomyces lanuginosus strain IMI 158749
-
-
Manually annotated by BRENDA team
member of glycosyl hydrolase family 5
UniProt
Manually annotated by BRENDA team
member of glycosyl hydrolase family 5
UniProt
Manually annotated by BRENDA team
; strain FTCC 5003
-
-
Manually annotated by BRENDA team
commercial preparations
-
-
Manually annotated by BRENDA team
strain gr
-
-
Manually annotated by BRENDA team
stran BK01
UniProt
Manually annotated by BRENDA team
Aspergillus niger BK01
stran BK01
UniProt
Manually annotated by BRENDA team
Aspergillus niger FTCC
strain FTCC 5003
-
-
Manually annotated by BRENDA team
Aspergillus niger FTCC 5003
-
-
-
Manually annotated by BRENDA team
strain CGMCC 1416
UniProt
Manually annotated by BRENDA team
strain CGMCC1554
Uniprot
Manually annotated by BRENDA team
Bacillus circulans CGMCC
strain CGMCC 1416
UniProt
Manually annotated by BRENDA team
Bacillus circulans CGMCC1554
strain CGMCC1554
Uniprot
Manually annotated by BRENDA team
gene name ydhT
UniProt
Manually annotated by BRENDA team
M-I, M-II, M-III
-
-
Manually annotated by BRENDA team
strain MSK-5
-
-
Manually annotated by BRENDA team
strain N16-5
-
-
Manually annotated by BRENDA team
Bacillus sp. MSK-5
strain MSK-5
-
-
Manually annotated by BRENDA team
strain N16-5
-
-
Manually annotated by BRENDA team
beta-mannanase; strain MA139
UniProt
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
isoform BCman-GH26
Uniprot
Manually annotated by BRENDA team
strain B36
-
-
Manually annotated by BRENDA team
strain WY34, induced by growth on konjac powder as carbon source at 50C
-
-
Manually annotated by BRENDA team
Bacillus subtilis B36
strain B36
-
-
Manually annotated by BRENDA team
Bacillus subtilis KK01
KK01
-
-
Manually annotated by BRENDA team
Bacillus subtilis KU-1
KU-1
-
-
Manually annotated by BRENDA team
Bacillus subtilis MA139
beta-mannanase; strain MA139
UniProt
Manually annotated by BRENDA team
Bacillus subtilis WY34
strain WY34, induced by growth on konjac powder as carbon source at 50C
-
-
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
Bispora sp.
strain MEY-1
UniProt
Manually annotated by BRENDA team
Caldicellulosiruptor sp.
Rt8B.4
-
-
Manually annotated by BRENDA team
Cellulosimicrobium sp.
member of glycosyl hydrolase family 5
UniProt
Manually annotated by BRENDA team
member of glycosyl hydrolase family 5
UniProt
Manually annotated by BRENDA team
member of glycoyl hydrolase family 26
-
-
Manually annotated by BRENDA team
isozymes ManA, ManB with at least 7 isomers
-
-
Manually annotated by BRENDA team
Dictyoglomus thermophilum Rt46B.1
Rt46B.1
-
-
Manually annotated by BRENDA team
Fusicoccum sp.
-
-
-
Manually annotated by BRENDA team
Gyoerffyella speciosa
-
-
-
Manually annotated by BRENDA team
isoform MAN1
Uniprot
Manually annotated by BRENDA team
Lilium testaceum
-
-
-
Manually annotated by BRENDA team
blue mussel
Uniprot
Manually annotated by BRENDA team
isozymes ManA, ManB
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
harboring a manA-containing plasmid
-
-
Manually annotated by BRENDA team
Orpinomyces sp.
strain PC-2
-
-
Manually annotated by BRENDA team
strain GS01, enzyme belongs to glycosyl hydrolase family 26. Protein additionally contains a glycosyl hydroxylase family 44 catalytic domain, a fibronectin domain type 3, and a cellulose-binding module type 3
-
-
Manually annotated by BRENDA team
Paenibacillus polymyxa GS01
strain GS01, enzyme belongs to glycosyl hydrolase family 26. Protein additionally contains a glycosyl hydroxylase family 44 catalytic domain, a fibronectin domain type 3, and a cellulose-binding module type 3
-
-
Manually annotated by BRENDA team
sequence consists of a carbohydrate binding module belonging to family 6 and a family 26 catalytic domain
UniProt
Manually annotated by BRENDA team
sequence consists of a carbohydrate binding module belonging to family 6 and a family 26 catalytic domain
UniProt
Manually annotated by BRENDA team
Penicillium occitanis Pol6
Pol6
-
-
Manually annotated by BRENDA team
Penicillium wortmanni
-
-
-
Manually annotated by BRENDA team
ATCC 43812
Swissprot
Manually annotated by BRENDA team
var. Mill.
Swissprot
Manually annotated by BRENDA team
Thermotoga neapolitana 5068
5068
-
-
Manually annotated by BRENDA team
Tyromyces palustris
-
-
-
Manually annotated by BRENDA team
strain MA-138
-
-
Manually annotated by BRENDA team
strain MA-138
UniProt
Manually annotated by BRENDA team
strain MA-138
-
-
Manually annotated by BRENDA team
strain MA-138
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Cellulosimicrobium sp.
G3FBL1
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
Q9FJZ3, Q9LZV3, Q9M0H6
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
-
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)
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4-beta-D-mannan + H2O
?
show the reaction diagram
B6V876
-
-
-
?
1,4-beta-D-mannan + H2O
?
show the reaction diagram
O05512
-
-
-
?
1,4-beta-D-mannan + H2O
?
show the reaction diagram
Aspergillus niger BK01
B6V876
-
-
-
?
2,4-dinitrophenyl-beta-mannobioside + H2O
2,4-dinitrophenol + beta-mannobiose
show the reaction diagram
-
-
-
-
?
azurine-crosslinked galactomannan + H2O
?
show the reaction diagram
-
hydrolysis
-
-
?
beta-1,4-D-mannan + H2O
?
show the reaction diagram
D0UHB3
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-mannotriose + beta-1,4-mannotetraose
show the reaction diagram
-
-
-
-
?
birch wood xylan + H2O
?
show the reaction diagram
Aspergillus niger, Aspergillus niger BK01
B6V876
9.1% of the activity with locust bean gum
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis WY34
-
poor substrate
-
-
?
carob galactomannan + H2O
?
show the reaction diagram
B6V876
-
-
-
?
carob-galactomannan + H2O
?
show the reaction diagram
P49425
i.e. locust bean gum
-
-
?
copra mannan + H2O
?
show the reaction diagram
-
90% of the activity with locust bean gum
-
-
?
copra meal defatted with n-hexane + H2O
?
show the reaction diagram
-
better substrate than locust bean gum and guar gum
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + oligosaccharide
[3H]-labelled polysaccharide
show the reaction diagram
-
transglucosylation
-
-
?
galactomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactomannan + H2O
?
show the reaction diagram
Q8L5J1
-
-
-
?
galactomannan + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis MA139
B5LX62
-
-
-
?
galactomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
Q0PQY8
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
Dictyoglomus thermophilum Rt46B.1
-
-
-
-
?
galactomannan + H2O
galactosyl-mannosyl oligosaccharides
show the reaction diagram
Q2I011
-
products show a degree of polymerization of 2-6
-
?
galactomannan + H2O
galactosyl-mannosyl oligosaccharides
show the reaction diagram
-
enzyme prefers galactomannans with lower degree of galactosylation e.g. from carob gum
-
-
?
galactomannan + H2O
galactosyl-mannosyl oligosaccharides
show the reaction diagram
-
source of substrate locust bean gum
-
-
?
glucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
glucomannan + H2O
?
show the reaction diagram
Q8L5J1
-
-
-
?
glucomannan + H2O
?
show the reaction diagram
B6V876
-
-
-
?
glucomannan + H2O
?
show the reaction diagram
O05512
-
-
-
?
glucomannan + H2O
?
show the reaction diagram
Q5PSP8
from konjac flour
-
-
?
glucomannan + H2O
?
show the reaction diagram
B5BQ69
from konjac flour
-
-
?
glucomannan + H2O
?
show the reaction diagram
Bispora sp.
B5LXD7
from konjac flour
70% of the activity with locust bean gum
-
?
glucomannan + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
D0UHB3
219% of the activity with locust bean gum
-
-
?
glucomannan + H2O
?
show the reaction diagram
Aspergillus niger BK01
B6V876
-
-
-
?
glucomannan + H2O
?
show the reaction diagram
Bacillus sp. MSK-5
-
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
?
show the reaction diagram
B5BQ69
from konjac flour
-
-
?
glucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
Lilium testaceum
-
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
Q0PQY8
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
of various size
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
Tyromyces palustris
-
-
of various size
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
glucosyl-mannosyl oligosaccharides
show the reaction diagram
Q2I011
-
products show a degree of polymerization of 2-6
-
?
glucomannan + H2O
glucosyl-mannosyl oligosaccharides
show the reaction diagram
-
source of substrate konjac
-
-
?
guar gum + H2O
mannose + mannobiose + mannotriose
show the reaction diagram
Talaromyces funiculosus, Penicillium wortmanni
-
-
-
-
guar gum + H2O
mannose + mannobiose + mannotriose
show the reaction diagram
-
-
mannobiose + mannotriose + mannotetraose
-
guar gum + H2O
?
show the reaction diagram
-
-
-
-
?
guar gum + H2O
?
show the reaction diagram
-
-
-
-
?
guar gum + H2O
?
show the reaction diagram
P49425
-
-
-
?
guar gum + H2O
?
show the reaction diagram
-
-
-
-
?
guar gum + H2O
?
show the reaction diagram
Bispora sp.
B5LXD7
-
14.8% of the activity with locust bean gum
-
?
guar gum + H2O
?
show the reaction diagram
Q49HI4
-
26% of the activity with locust bean gum
-
?
guar gum + H2O
?
show the reaction diagram
-
21% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
show the reaction diagram
B6V876
18% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
show the reaction diagram
-
90% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
show the reaction diagram
Aspergillus niger BK01
B6V876
18% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
show the reaction diagram
Bacillus circulans CGMCC
Q49HI4
-
26% of the activity with locust bean gum
-
?
guar gum + H2O
?
show the reaction diagram
Bacillus subtilis B36
-
21% of the activity with locust bean gum
-
-
?
guar gum galactomannan + H2O
?
show the reaction diagram
-
-
-
-
?
guar gum glucomannan + H2O
?
show the reaction diagram
Q5AZ53, Q5B7X2
-
-
-
?
guar gum glucomannan + H2O
?
show the reaction diagram
Q5AZ53, Q5B7X2
-
-
-
?
ivory nut mannan + H2O
mannobiose + mannotriose
show the reaction diagram
-
-
-
?
ivory nut mannan + H2O
?
show the reaction diagram
Q5PSP8
-
-
-
?
ivory nut mannan + H2O
?
show the reaction diagram
-
-
-
-
?
ivory nut mannan + H2O
?
show the reaction diagram
Q00012
-
-
-
?
ivory nut mannan + H2O
mannotriose + mannotetraose + mannopentaose + mannohexaose
show the reaction diagram
Cellulosimicrobium sp., Cellulosimicrobium sp. HY-13
G3FBL1
-
main products, at 14%, 25%, 20%, and 13%, respectively
-
?
konjac glucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
konjac glucomannan + H2O
?
show the reaction diagram
Q5AZ53, Q5B7X2
-
-
-
?
konjac glucomannan + H2O
?
show the reaction diagram
C6KL35
-
-
-
?
konjac glucomannan + H2O
?
show the reaction diagram
Q5AZ53, Q5B7X2
-
-
-
?
konjac glucomannan + H2O
?
show the reaction diagram
C6KL35
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
Bacillus subtilis KK01
-
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Q5PSP8
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Q0PQY8
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Q2LE69
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
B4XC07
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Bispora sp.
B5LXD7
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
C6KL35
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Q0IJR6
-
76% of products are oligomannosides
-
?
locust bean gum + H2O
?
show the reaction diagram
Q49HI4
-
hydrolysis products are mainly oligosaccharides plus one monosaccharide
-
?
locust bean gum + H2O
?
show the reaction diagram
D0UHB3
-
main products are manno-oligosaccharides of 2-6 residues and mannose
-
?
locust bean gum + H2O
?
show the reaction diagram
O05512
-
products are various manno-oligosaccharides of M2-M6 size and mannose
-
?
locust bean gum + H2O
?
show the reaction diagram
-
enzyme is highly specific for substrate
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Paenibacillus polymyxa GS01
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Bacillus sp. MSK-5
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Penicillium occitanis Pol6
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
C6KL35
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Bacillus circulans CGMCC
Q49HI4
-
hydrolysis products are mainly oligosaccharides plus one monosaccharide
-
?
locust bean gum + H2O
?
show the reaction diagram
Bacillus subtilis WY34
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Bacillus subtilis B36
-
enzyme is highly specific for substrate
-
-
?
locust bean gum + H2O
mannopentaose
show the reaction diagram
Cellulosimicrobium sp., Cellulosimicrobium sp. HY-13
G3FBL1
-
44%, main product
-
?
locust bean gum galactomannan + H2O
mannobiose
show the reaction diagram
B6V876
-
main product, with low amounts of mannotirose and higher manno-oligosaccarides
-
?
locust bean gum glucomannan + H2O
?
show the reaction diagram
Q5AZ53, Q5B7X2
-
-
-
?
locust bean gum glucomannan + H2O
?
show the reaction diagram
Q5AZ53, Q5B7X2
-
-
-
?
low viscosity locust bean galactomannan + H2O
?
show the reaction diagram
-
-
-
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
2 Man-beta-1,4-Man
show the reaction diagram
Q5AZ53, Q5B7X2
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
show the reaction diagram
Q5AZ53, Q5B7X2
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
show the reaction diagram
Q5AZ53, Q5B7X2
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
show the reaction diagram
Q5AZ53, Q5B7X2
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
show the reaction diagram
Q5AZ53, Q5B7X2
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
show the reaction diagram
Q5AZ53, Q5B7X2
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
show the reaction diagram
Q5AZ53, Q5B7X2
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
show the reaction diagram
Q5AZ53, Q5B7X2
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)Man + H2O
?
show the reaction diagram
-
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Man + H2O
mannose + Manbeta(1-4)Man
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + mannose + Manbeta(1-4)Man
show the reaction diagram
Q8WPJ2
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
mannose + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Man
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
Q8L5J1
-
-
-
?
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
show the reaction diagram
Q8WPJ2
-
-
-
?
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
show the reaction diagram
Q2I011
-
-
-
-
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
Q8WPJ2
-
-
-
?
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
show the reaction diagram
Q8WPJ2
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
Q8WPJ2
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
-
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
-
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
Q0PQY8
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
dimers, trimers and other
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
codium, coffee
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
Bacillus subtilis KK01
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
-
mannan + H2O
?
show the reaction diagram
-
-
-
-
?
mannan + H2O
?
show the reaction diagram
Q8L5J1
-
-
-
?
mannan + H2O
mannosyl oligosaccharides
show the reaction diagram
Q2I011
-
products show a degree of polymerization of 2-6
-
?
mannan + H2O
mannotetraose + mannobiose + mannotriose
show the reaction diagram
Bacillus subtilis, Bacillus subtilis WY34
-
source of substrate: copra
-
-
?
mannan A + H2O
?
show the reaction diagram
-
-
-
-
?
mannohexaose + H2O
mannotriose
show the reaction diagram
-
-
main product
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannotriose + mannobiose
show the reaction diagram
-
-
main products
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
small amounts of mannose and mannotriose
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
small amounts of mannose and mannotriose
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
small amounts of mannose and mannotriose
?
mannotriose + H2O
mannobiose + mannose
show the reaction diagram
-
-
-
?
mannotriose + H2O
mannobiose + mannose
show the reaction diagram
-
-
-
?
mannotriose + H2O
mannobiose + mannose
show the reaction diagram
-
-
-
?
palm kernel cake + H2O
?
show the reaction diagram
Aspergillus niger, Aspergillus niger FTCC 5003, Aspergillus niger FTCC
-
-
-
-
?
starch + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis WY34
-
poor substrate
-
-
?
tara gum galactomannan + H2O
?
show the reaction diagram
-
-
-
-
?
xylan + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis WY34
-
poor substrate
-
-
?
mannotriose + H2O
mannobiose + mannose
show the reaction diagram
-
-
not
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
not: mannobiose
-
-
?
additional information
?
-
-
not: mannobiose
-
-
?
additional information
?
-
-
not: mannobiose
-
-
?
additional information
?
-
-
transglycosylation reaction, Streptomyces: transfer of one mannose unit from oligosaccharides, fenugreek: transfer of oligomannose residues
-
-
-
additional information
?
-
-
no substrate: mannotriose, mannobiose, enzyme requires a minimum of four sugar units in substrates
-
-
-
additional information
?
-
-
no substrate: xylan, caroxymethyl cellulose, cellulose, mannan
-
-
-
additional information
?
-
P49425
requires at least five sugar moieties for effective catalytic activity, no substrate: yeast mannan
-
-
-
additional information
?
-
Q2I011
during hydrolysis of 1,4-beta-manno-oligosaccharides, transglycosylation reactions occur
-
-
-
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
?
-
Q0PQY8
enzyme exhibits substantial transglycosylase activity
-
-
-
additional information
?
-
-
no substrate: carboxymethyl cellulose
-
-
-
additional information
?
-
B5BQ69
enzyme has the ability to bind soluble beta-mannans, 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
?
-
Q49HI4
no substrate: soluble starch, methylcellulose
-
-
-
additional information
?
-
Q5PSP8
no substrates: mannobiose, mannotriose, mannotetraose, mannohexaose
-
-
-
additional information
?
-
B6V876
negligible activity with starch, carboxymethyl cellulose, and alpha-cellulose
-
-
-
additional information
?
-
-
no substrate: carboxymethyl cellulose, oat spelt xylan, starch, pectin, 4-nitrophenyl-beta-D-mannopyranoside
-
-
-
additional information
?
-
-
enzyme is active in hydrolyzing the beta-mannan-rich cell wall of soybean seeds
-
-
-
additional information
?
-
Q5AZ53, Q5B7X2
enzyme displays good transgycosylation activity using mannotriose, melezitose and isomaltotriose as acceptors
-
-
-
additional information
?
-
Q5AZ53, Q5B7X2
enzyme displays transglycosylation activity using only mannotriose as acceptor
-
-
-
additional information
?
-
O05512
no substrate: guar gum, copra meal
-
-
-
additional information
?
-
Cellulosimicrobium sp.
G3FBL1
no substrate: mannobiose, or 4-nitrophenyl sugar derivatives
-
-
-
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
?
-
G3FBL1
no substrate: mannobiose, or 4-nitrophenyl sugar derivatives
-
-
-
additional information
?
-
Aspergillus niger BK01
B6V876
negligible activity with starch, carboxymethyl cellulose, and alpha-cellulose
-
-
-
additional information
?
-
Dictyoglomus thermophilum Rt46B.1
-
-
-
-
?
additional information
?
-
Q5AZ53, Q5B7X2
enzyme displays good transgycosylation activity using mannotriose, melezitose and isomaltotriose as acceptors
-
-
-
additional information
?
-
Q5AZ53, Q5B7X2
enzyme displays transglycosylation activity using only mannotriose as acceptor
-
-
-
additional information
?
-
Penicillium occitanis Pol6
-
no substrate: carboxymethyl cellulose, oat spelt xylan, starch, pectin, 4-nitrophenyl-beta-D-mannopyranoside
-
-
-
additional information
?
-
B5BQ69
enzyme has the ability to bind soluble beta-mannans, 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
?
-
Bacillus circulans CGMCC
Q49HI4
no substrate: soluble starch, methylcellulose
-
-
-
additional information
?
-
Bacillus subtilis B36
-
no substrate: carboxymethyl cellulose
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
guar gum + H2O
mannose + mannobiose + mannotriose
show the reaction diagram
Talaromyces funiculosus, Penicillium wortmanni
-
-
-
-
guar gum + H2O
mannose + mannobiose + mannotriose
show the reaction diagram
-
-
mannobiose + mannotriose + mannotetraose
-
ivory nut mannan + H2O
mannobiose + mannotriose
show the reaction diagram
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
Bacillus subtilis KK01
-
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
?
mannan + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme is active in hydrolyzing the beta-mannan-rich cell wall of soybean seeds
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ag+
Bispora sp.
B5LXD7
stimulation
Ca2+
-
stimulates
Ca2+
B4XC07
5 mM, 228% of initial activity
Ca2+
Q49HI4
1 mM, 124% of initial activity
Ca2+
-
2.5 mM, 10% stimulation. Inhibition at 2.0 mM
Ca2+
Q8P9S0
1 mM, 119% of initial activity
Co2+
-
1 mM, 126% of initial activity
Co2+
Q49HI4
1 mM, 112% of initial activity
Cu2+
B4XC07
5 mM, 151% of initial activity
Cu2+
-
2.5 mM, 9% stimulation
Cu2+
B5LX62
38% residual activity
Cu2+
B6V876
110% of initial activity
EDTA
B5LX62
64% residual activity
Fe2+
-
1 mM, 124% of initial activity
Fe3+
Bispora sp.
B5LXD7
stimulation
Li+
Q49HI4
1 mM, 112% of initial activity
Mg2+
-
slight activation
Mg2+
B4XC07
5 mM, 178% of initial activity
Mg2+
Q8P9S0
1 mM, 118% of initial activity
Mn2+
Bispora sp.
B5LXD7
stimulation
Mn2+
B5LX62
53% residual activity
Ni2+
Bispora sp.
B5LXD7
stimulation
Pb2+
C6KL35
slight stimulation
Zn2+
B4XC07
5 mM, 220% of initial activity
Zn2+
B5LX62
79% residual activity
Zn2+
C6KL35
slight stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
C6KL35
1 mM, 54% residual activity
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
Ag+
-
1 mM, 54% residual activity
Ag+
-
1 mM, complete loss of activity
Ag+
-
1 mM, 3% residual activity
Ag+
Q0IJR6
strong inhibition
Ag+
-
90% inhibition
Ag+
B5BQ69
1 mM, more than 80% inhibition
Ag+
B4XC07
5 mM, 24.8% residual activity
Ag+
Q49HI4
1 mM, 2% residual activity
Ag+
Q8P9S0
1 mM, 18% residual activity
Ag+
-
complete inhibition
Ag+
-
48% residual activity
Al3+
B5BQ69
1 mM, more than 80% inhibition
Al3+
Q8P9S0
1 mM, 31% residual activity
Ca2+
-
2 mM, 64% residual activity. Stimulating above 2.5 mM
Ca2+
C6KL35
1 mM, 83% residual activity
Co2+
-
1 mM, 50% loss of activity
Co2+
-
2.5 mM, 42% residual activity
Cu2+
-
1 mM, 49% loss of activity
Cu2+
-
35-40% inhibition
Cu2+
B5BQ69
1 mM, more than 80% inhibition
Cu2+
Q49HI4
1 mM, 12% residual activity
Cu2+
Q8P9S0
1 mM, 2% residual activity
Cu2+
-
complete inhibition
Cu2+
Cellulosimicrobium sp.
G3FBL1
more than 50% inhibtion
Cu2+
C6KL35
1 mM, 76% residual activity
dithiothreitol
-
1 mM, 25% loss of activity
EDTA
-
1 mM, 37% residual activity
EDTA
-
1 mM, 33.9% residual activity
EDTA
-
2.5 mM, 77% residual activity
EDTA
Cellulosimicrobium sp.
G3FBL1
5 mM, 20% residaul activity
Fe2+
-
1 mM, 40% loss of activity
Fe2+
Cellulosimicrobium sp.
G3FBL1
more than 50% inhibtion
Fe3+
-
90% inhibition
Fe3+
-
2.5 mM, 71% residual activity
Fe3+
Q8P9S0
1 mM, 37% residual activity
Fe3+
-
30.6% residual activity
Hg2+
-
1 mM, 2% residual activity
Hg2+
Q0IJR6
strong inhibition
Hg2+
Bispora sp.
B5LXD7
strong
Hg2+
B5BQ69
1 mM, more than 80% inhibition
Hg2+
B4XC07
5 mM, 16.4% residual activity
Hg2+
Q49HI4
1 mM, 8% residual activity
Hg2+
Q8P9S0
1 mM, 1% residual activity
Hg2+
-
complete inhibition
Hg2+
C6KL35
1 mM, 4% residual activity
K+
C6KL35
1 mM, 62% residual activity
Mg2+
-
1 mM, 53% residual activity
Mg2+
-
84% residual activity
Mn2+
-
1 mM, 22% residual activity
Mn2+
-
35-40% inhibition
Mn2+
B4XC07
5 mM, 32% residual activity
Mn2+
B6V876
35% of initial activity
Mn2+
-
5 mM, 50% residual activity
N-bromosuccinimide
-
-
N-bromosuccinimide
-
1 mM, 3% residual activity
N-bromosuccinimide
-
complete inhibition
Ni2+
-
1 mM, 61% residual activity
p-chloromercuribenzoate
-
-
Pb2+
B5BQ69
1 mM, more than 80% inhibition
Sodium dodecyl sulfate
Q0IJR6
strong inhibition
Sodium dodecyl sulfate
Bispora sp.
B5LXD7
strong
Sodium dodecyl sulfate
B6V876
20% of initial activity
sodium dodecylsulfate
-
1 mM, 55% residual activity
sodium dodecylsulfate
-
1 mM, 79% residual activity
Zn2+
B5BQ69
1 mM, more than 80% inhibition
Zn2+
Q8P9S0
1 mM, 16% residual activity
Zn2+
-
68% residual activity
Zn2+
Cellulosimicrobium sp.
G3FBL1
more than 50% inhibtion
Mn2+
C6KL35
1 mM, 63% residual activity
additional information
-
not inhibitory: EDTA, 2-mercaptoethanol
-
additional information
Bispora sp.
B5LXD7
enzymatic activity is not significantly affected by ions such as Ca2+, Cr3+, Co2+, Zn2+, Na+, K+, and Mg2+
-
additional information
-
not inhibitory: EDTA, phenyl methyl sulfonyl fluoride, 1,10-phenanthroline
-
additional information
C6KL35
not inhibtory: Mg2+, Co2+, EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
1 mM, 11% increase in activity
2-mercaptoethanol
Q8P9S0
1 mMm, 121% of initial activity
2-mercaptoethanol
-
153% of initial activity
Ca2+
-
1 mM, 20% increase in activity
cysteine
-
slight activation
dithiothreitol
-
129% of initial activity
Sodium azide
Cellulosimicrobium sp.
G3FBL1
hydrolysis of locust bean gum is enhanced by approximately 1.45fold in poresence of sodium azide
Triton X-100
Q8P9S0
1%, 123% of initial activity
EDTA
B6V876
236% of initial activity
additional information
-
an assembly of ManB with mini-CbpA, which contains a carbohydrate-binding module that provides proximity to insoluble substrates, increases the activity toward galactomannan from locust bean gum and guar gum 1.7- and 2.0fold over those without mini-CbpA
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
1.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
wild-type, pH 5.5, 37C
2.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
2.9
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
pH 5.5, 37C
0.6
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
wild-type, pH 5.5, 37C
1
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
1.3
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
1.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
pH 5.5, 37C
9
Manbeta(1-4)Manbeta(1-4)Man
-
-
2.49
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Q8WPJ2
-
1.61
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Q8WPJ2
-
5.3
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Q2I011
30C, pH 4.8
1.9
soluble mannan
-
-
-
0.04
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant H143A
additional information
locust bean gum
-
KM value is 34.9 mg/ml, pH 5.0, 28C
-
additional information
locust bean gum
C6KL35
KM value is 3.8 mg/ml
-
0.5
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Q8WPJ2
-
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
-
-
-
additional information
additional information
Q2I011
Km value is 0.16 mg/ml for locust-bean galactomannan
-
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
Q0PQY8
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
Q2LE69
Km value for locust bean gum at pH 2.4, 50C is 0.93 mg/ml
-
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
B5BQ69
Km value for konjac glucomannan 0.6 mg/ml
-
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
B6V876
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
D0UHB3
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
148
1,4-beta-D-Mannan
B6V876
70C
18200
beta-1,4-D-mannan
D0UHB3
50C, pH 6.0
292
carob galactomannan
B6V876
70C
-
12.9
galactomannan
Q2I011
30C, pH 4.8
-
215
glucomannan
B6V876
70C
21000
glucomannan
D0UHB3
50C, pH 6.0
25.2
locust bean gum
-
pH 5.0, 28C
-
31200
locust bean gum
D0UHB3
50C, pH 6.0
-
330
locust bean gum galactomannan
B6V876
70C
-
1935
low viscosity locust bean galactomannan
-
isozyme MAN I
-
2246
low viscosity locust bean galactomannan
-
isozyme MAN II
-
2.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
67
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
pH 5.5, 37C
98
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
112
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
wild-type, pH 5.5, 37C
117
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
134
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
wild-type, pH 5.5, 37C
148
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
193
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
pH 5.5, 37C
1.17
Manbeta(1-4)Manbeta(1-4)Man
-
-
0.41
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
-
-
0.7
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Q8WPJ2
-
11.64
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
-
-
0.26
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
-
-
3.9
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Q2I011
30C, pH 4.8
45
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Q8WPJ2
-
52.42
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
-
-
77
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
-
-
99
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Q8WPJ2
-
additional information
additional information
Q5PSP8
turnover numbers are 61.2 per s, substrate locust bean gum, wild-type, 75.1 per s, konjac flour, wild-type, 11 per s, ivory nut mannan, wild-type, 1.97 per s, locust bean gum, mutant E167A, 26.5 per s, locust bean gum, mutant H1A/H23A, respectively, at 37C, pH 7.0
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
23
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
pH 5.5, 37C
7928
27
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
7928
36
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
7928
61
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
wild-type, pH 5.5, 37C
7928
109
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
pH 5.5, 37C
8926
115
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
8926
118
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
8926
215
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Q5AZ53, Q5B7X2
wild-type, pH 5.5, 37C
8926
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.69
-
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man}
1.13
-
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
1.95
-
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
2.2
-
substrate guar gum, pH 7.0, 40C
3.1
-
Manbeta(1-4)Manbeta(1-4)Man
4.6
-
crude medium
4.8
-
pH 7.0, 30C, substrate beta-1,4-mannan
9.6
-
pH 7.0, 30C, substrate glucomannan
11.48
-
pH 7.0, 30C, substrate galactomannan
12.2
-
substrate locust bean gum, pH 7.0, 40C
18.5
-
substrate glucomannan, pH 7.0, 40C
27.4
-
pH 7.0, 30C
45.7
-
isozyme MAN I, after 9.9fold purification with DEAE Sepharose chromatography
56.7
-
isozyme MAN II, after 12.3fold purification with DEAE Sepharose chromatography
64.6
Q00012
pH 5.0, 50C, recombinant protein
129.3
-
pH 4.0, 40C
190
-
isozyme MAN I, mannan A
215
-
isozyme MAN II, mannan A
225.4
-
isozyme MAN II, after 49fold purification with Phenyl Sepharose chromatography
264.1
Q00012
pH 5.0, 50C, native protein
294
-
isozyme MAN I, guar gum
317
-
isozyme MAN II, guar gum
366
Q2LE69
pH 2.4, 50C
380
-
41.9 kDa protein
416.3
B4XC07
30C, pH 3.5
471
-
isozyme MAN I, after 102.4fold purification with Phenyl Sepharose chromatography
475
-
61.2 kDa protein
481.5
Q49HI4
-
562
-
isozyme MAN I, locust bean gum
627
-
isozyme MAN II, locust bean gum
635
O05512
pH 6.0, 60C, substrate locust bean gum
663
-
isozyme MAN I, low viscosity locust bean galactomannan
751
-
isozyme MAN II, low viscosity locust bean galactomannan
928
-
pH 6.4, 50C
962
O05512
pH 6.0, 60C, substrate glucomannan
1139
-
pH 5.0, 40C
1400
-
ManB, 37C, pH 5.0
1672
D0UHB3
50C, pH 6.0
2223
O05512
pH 6.0, 60C, substrate 1,4-beta-D-mannan
3373
Bispora sp.
B5LXD7
pH 1.5, 65C
4839
Q0IJR6
pH 7.6, 60C
5383
-
50C
8302
-
pH 6.0, 50C
8498
Cellulosimicrobium sp.
G3FBL1
substrate locust bean gum, pH 6.0, 50C
14710
Cellulosimicrobium sp.
G3FBL1
substrate ivory nut mannan, pH 6.0, 50C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
1638 A550/min/mg optical path 1cm,isozyme MAN I, OBR-LBG; 1763 A550/min/mg optical path 1cm, isozyme MAN II, OBR-LBG; no activity against 4-nitrophenyl-alpha and -beta-mannopyranosides
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.9
-
61.2 kDa protein
3.3
-
41.9 kDa protein
3.5 - 4.5
-
-
4 - 6
Q0PQY8
broad
4.5 - 5
B6V876
-
4.5 - 5.5
-
-
4.5
Lilium testaceum
-
-
4.5
Q4WBS1
recombinant enzyme expressed in Aspergillus sojae
4.5
C6KL35
-
4.8
Q2I011
-
5
-
recombinant protein
5
-
xylanase and mannanase activities of enzyme
5.2
Q4WBS1
recombinant enzyme expressed in Pichia pastoris
5.5
Q5AZ53, Q5B7X2
;
6
Penicillium wortmanni
-
-
6
Cellulosimicrobium sp.
G3FBL1
-
6.5
-
-
7
B5BQ69
-
7.5
-
-
8.5
-
M-III, at 65C
9
-
M-I, M-II, at 60C
11.5
Bispora sp.
B5LXD7
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 5.5
Bispora sp.
B5LXD7
more than 70% of maximum activity within
2.2 - 8
Q2LE69
-
2.5 - 6
B4XC07
more than 50% of maximum activity
3 - 8
-
pH 3: 15% of maximal activity
3 - 9
B5LX62
more than 60% of maximum activity
4 - 7.5
-
-
4 - 8.5
C6KL35
-
4.5 - 7
Q5AZ53, Q5B7X2
more than 95% of maximum activity; more than 95% of maximum activity
5 - 8
-
more than 70% of maximum activity
6 - 10
-
-
6
E5RSM0
rapid loss of activity above, recombinant enzyme
6.8 - 8
Q49HI4
more than 75% of maximum activity
7 - 8
Q0IJR6
more than 75% of maximum activity within
7.5
E5RSM0
rapid loss of activity above, native enzyme
8
B5LX62
50% of maximum activity
10
-
44% of maximum activity
additional information
Penicillium wortmanni
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
Lilium testaceum
-
-
40
Q8WPJ2
-
45
Q4WBS1
recombinant enzyme expressed in Pichia pastoris
45
E5RSM0
recombinant enzyme
50 - 60
-
for four enzyme forms
50 - 60
D0UHB3
-
50
B5BQ69
-
50
Q5AZ53, Q5B7X2
;
50
Cellulosimicrobium sp.
G3FBL1
-
60
-
M-I, M-II
60
-
recombinant protein from Aspergillus oryzae, SDS-PAGE
60
-
at pH 4.5
60
Q4WBS1
recombinant enzyme expressed in Aspergillus sojae
65
-
M-III
65
Bispora sp.
B5LXD7
-
72
-
41.9 kDa protein
74
-
61.2 kDa protein
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 5
B4XC07
20-40% of maximum activity
5 - 60
-
recombinant enzyme, more than 30% of maximum activity within
20 - 30
-
more than 80% of maximum activity
30 - 70
Penicillium wortmanni
-
-
30 - 80
-
30C: about 25% of maximal activity, 80C: about 30% of maximal activity
35 - 65
C6KL35
-
40
B5LX62
about 50% of maximum activity
50 - 55
-
-
50 - 70
-
-
50
-
rapid decrease in activity above
70
C6KL35
40% of maximum activity
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
-
isoelectric focusing
4.6 - 4.7
Q8L5J1
calculated from amino acid sequence
4.6
Cellulosimicrobium sp.
G3FBL1
calculated
4.75 - 4.9
-
isozyme MAN II
4.9 - 5.2
-
isozyme MAN I
4.9
Q2LE69
isoelectric focusing
5.5
-
chromatofocusing, 7 isomers
5.5
-
calculated
6.9
-
isoelectric focusing
7.8
Q2I011
isoelectric focusing
9
Q8L5J1
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Lilium testaceum
-
-
Manually annotated by BRENDA team
-
specifically expressed in cotyledons of seedling
Manually annotated by BRENDA team
Bacillus subtilis KU-1, Thermotoga neapolitana 5068, Bacillus subtilis KK01
-
-
-
Manually annotated by BRENDA team
Orpinomyces sp.
-
-
Manually annotated by BRENDA team
Bacillus sp. N16-5, Bacillus subtilis B36
-
-
-
Manually annotated by BRENDA team
Tyromyces palustris
-
-
Manually annotated by BRENDA team
Q8L5J1
red fruit, not during early stages of ripening
Manually annotated by BRENDA team
-
isoform Man4a is expressed in the fruit cell wall at all ripening stages, but it is not active during the initial green stage. This is not due to the presence of inhibitors of its activity, nor due to changes in its mRNA sequence
Manually annotated by BRENDA team
-
high degree of enzyme expression during germination facilitates radicle protrusion through the surrounding endosperm by weakeing it in the region close to the radicle tip
Manually annotated by BRENDA team
-
germinating
Manually annotated by BRENDA team
Q2I011
10 days old
Manually annotated by BRENDA team
-
specifically expressed in cotyledons of seedling
Manually annotated by BRENDA team
additional information
Q8L5J1
not in leaf
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q6YM50
main enzyme activity in the fruit
Manually annotated by BRENDA team
-
transient expression in onion epidermal cells of endo-beta-mannanase trancripts fused to green fluorescent protein results in the expressed enzyme being localized to the cell walls. This occurs initially during ripening in the skin and outer pericarp of the fruit, and later in the skin and throughout the pericarp
Manually annotated by BRENDA team
B6V876
recombinant enzyme
-
Manually annotated by BRENDA team
Aspergillus niger BK01
-
recombinant enzyme
-
-
Manually annotated by BRENDA team
Bacillus subtilis B36
-
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Cellvibrio japonicus (strain Ueda107)
Cellvibrio japonicus (strain Ueda107)
Cellvibrio japonicus (strain Ueda107)
Cellvibrio japonicus (strain Ueda107)
Cellvibrio japonicus (strain Ueda107)
Cellvibrio japonicus (strain Ueda107)
Cellvibrio japonicus (strain Ueda107)
Cellvibrio japonicus (strain Ueda107)
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18000
-
SDS-PAGE
707194
24000
-
gel filtration
208790
25000
-
gel filtration
208792, 208794
27000
-
gel filtration
208792, 208794
33000
Lilium testaceum
-
gel filtration
208803
36000
-
gel filtration
678989
37000
-
SDS-PAGE
208788
37000
-
SDS-PAGE
208798
38950
-
calculation from sequence of DNA
208805
39000
-
SDS-PAGE, 40000 by gel filtration
208809
39000
-
gel filtration, ManA and ManB
656335
39000
Q8WPJ2
method not mentioned
666074
39000
-
SDS-PAGE
666685
40000
-
-
208804
40000
-
-
208808
40000
Q8L5J1
SDS-PAGE
666855
41000
-
SDS-PAGE
208788, 208798
41000
-
recombinant protein expressed in E. coli, SDS-PAGE
208806
41900
-
-
136060
42000
-
M-III, SDS-PAGE
208796
43100
-
calculation from sequence of DNA
208806
44000
-
SDS-PAGE
208792, 208794
45000
-
-
208798
45000
-
recombinant protein expressed in Aspergillus oryzae, SDS-PAGE
208807
46000
-
SDS-PAGE
208784, 208787, 208799, 208800
49000
-
SDS-PAGE
208814
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
664068
53000
-
SDS-PAGE
208788
55000
-
-
208813
57000
-
SDS-PAGE
208795
58000
-
M-I, SDS-PAGE
208796
59000
-
M-II, SDS-PAGE
208796
60000
-
isozyme MAN I, SDS-PAGE
664167
61200
-
-
136060
63000
-
isozyme MAN II, SDS-PAGE
664167
65000
-
SDS-PAGE
136061
65000
-
PAGE
709495
70000
-
gel filtration
208792, 208794
70000
B5BQ69
gel fitlration
696843
162000
-
dimeric protein, SDS-PAGE
208816
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
B6V876
x * 53000, SDS-PAGE
?
-
x * 38000, SDS-PAGE
?
Q2I011
x * 43000, SDS-PAGE
?
-
x * 26000, SDS-PAGE
?
Q0PQY8
x * 65000, SDS-PAGE
?
-
x * 40000, SDS-PAGE
?
Q49HI4
x * 31000, SDS-PAGE
?
A5IMX7
x * 44000, SDS-PAGE
?
P49425
x * 113000, deduced from gene sequence, upon expression in Escherichia coli, two fragments of 45000 and 50000 Da
?
Q8L5J1
x * 42400, deduced from gene sequence, mature protein
?
-
x * 43000, ManB, SDS-PAGE
?
Q00012
x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
?
-
x * 37700, calculated
?
-
x * 145294, calculated
?
-
x * 38013, calculated, x * 38000, SDS-PAGE, mature protein
?
-
x * 39000, SDS-PAGE, x * 39627, calculated for mature protein
?
-
x * 39600, SDS-PAGE
?
Q2LE69
x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
?
Q0IJR6
x * 32000, calculated and SDS-PAGE
?
Bispora sp.
B5LXD7
x * 46800, SDS-PAGE
?
Q4WBS1
x * 60000, SDS-PAGE, recombinant enzyme
?
Q8P9S0
x * 33000, SDS-PAGE and calculated
?
D0UHB3
x * 45000, SDS-PAGE, x * 41000, calculated
?
E5RSM0
x * 39961, calculated
?
Cellulosimicrobium sp.
G3FBL1
x * 44000, SDS-PAGE, x * 43767, calculated
?
C6KL35
x * 53600, calculated
?
Q5AZ53, Q5B7X2
x * 56000, SDS-PAGE, x * 43847, calculated
?
Q5AZ53, Q5B7X2
x * 56000, SDS-PAGE, x * 46644, calculated
?
-
x * 70000, SDS-PAGE, recombinant protein including His-tag
?
-
x * 44000, SDS-PAGE, x * 43767, calculated
-
?
Aspergillus niger BK01
-
x * 53000, SDS-PAGE
-
?
-
x * 56000, SDS-PAGE, x * 43847, calculated, x * 56000, SDS-PAGE, x * 46644, calculated
-
?
Paenibacillus polymyxa GS01
-
x * 145294, calculated
-
?
Alicyclobacillus acidocaldarius Tc-12-31
-
x * 38000, SDS-PAGE
-
?
-
x * 53600, calculated
-
?
-
x * 37700, calculated
-
?
-
x * 44000, SDS-PAGE
-
?
Bacillus circulans CGMCC
-
x * 31000, SDS-PAGE
-
?
Bacillus subtilis WY34
-
x * 39600, SDS-PAGE
-
?
Bacillus subtilis B36
-
x * 38013, calculated, x * 38000, SDS-PAGE, mature protein
-
dimer
-
2 * 73000, SDS-PAGE
monomer
-
1 * 66000, SDS-PAGE
monomer
-
1 * 39216, ManA, 1 * 39265, ManB, MALDI-TOF spectrometry
monomer
B5BQ69
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
-
additional information
P49425
C-terminal domain of 550 amino acid residues with homology to glycosidase family 26
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
E5RSM0
sequence contains a N-terminal signal peptide of 17 amino acids
glycoprotein
Q00012
treatment with PNGaseF results in a shift to 41000 Da, both for native and recombinant protein
glycoprotein
Q5AZ53, Q5B7X2
treatment by endoglycosidase H decreases molecular mass to 46000 Da
glycoprotein
Q5AZ53, Q5B7X2
treatment by endoglycosidase H decreases molecular mass to 51000 Da
glycoprotein
-
treatment by endoglycosidase H decreases molecular mass to 51000 Da, treatment by endoglycosidase H decreases molecular mass to 46000 Da
-
glycoprotein
B6V876
-
glycoprotein
Aspergillus niger BK01
-
-
-
glycoprotein
Q2LE69
treatment with Endo H leads to 30% loss of enzymic activity and a reduction in molecular weight by about 9 kDa
glycoprotein
-
carbohydrate content of 13.1%
glycoprotein
Bacillus subtilis WY34
-
carbohydrate content of 13.1%
-
proteolytic modification
Cellulosimicrobium sp.
G3FBL1
sequence contains a N-terminal signal peptide of 24 amino acids
proteolytic modification
-
sequence contains a N-terminal signal peptide of 24 amino acids
-
glycoprotein
-
two putative N-glycosilation sites, ManB
proteolytic modification
-
sequence contains a signal peptide of 17 amino acids
glycoprotein
-
5% carbohydrate content
glycoprotein
Penicillium occitanis Pol6
-
5% carbohydrate content
-
proteolytic modification
Q0PQY8
sequence contains a secretory signal peptide
glycoprotein
-
-
proteolytic modification
Q8L5J1
amino acid sequence contains a signal peptide cleavage site between residues 21-22, targeting sequence for cell wall
glycoprotein
-
-
proteolytic modification
B5BQ69
sequence contains a signal peptide of 26 amino acids
glycoprotein
-
-
-
proteolytic modification
-
sequence contains a signal peptide of 26 amino acids
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native and selenomethionyl enzyme, to 1.9 and 1.99 A resolution, respectively
-
to 1.45 A resolution, crystal shows a typical (beta/alpha)8 folding type. The catalytic acid/base Glu167 and nucleophile Glu266 are positioned on the beta4 and beta7 strands, respectively
Q5PSP8
hanging-drop vapor diffusion method at room temperature
-
both native protein and selenomethionyl derivative, enzyme expressed in Pichia pastoris
-
hanging drop vapor diffusion
Q8L5J1
molecular dynamic simulation of wild-type and mutant lacking the C-terminal amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein
-
recombinant enzyme
-
crystallization of catalytic domain. Crystals from conditions with phosphate or citrate salts as precipitant belong to space group P212121, resolution to 1.4 A, while a crystal from a condition with ethanol as precipitant belongs to space group I212121, resolution to 1.45 A
A5IMX7
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 10
O05512
50C, stable for 30 min
714384
2 - 12
-
-
707194
2.5 - 10
-
recombinant protein expressed in Aspergillus oryzae
208807
4 - 5
-
-
136060
4 - 8
-
40C, 1 h
208786, 208798
4 - 8
Q0PQY8
-
679584
4 - 9
-
-
656335
4
-
40C, 20 min, stable
714768
4.5 - 8
-
-
208795
4.5 - 8.5
-
-
664167
4.5 - 9
Caldicellulosiruptor sp.
-
-
208810
5 - 12
D0UHB3
after incubation at 50C for 30 min
709829
5 - 8
-
-
208798
5 - 9
-
-
208790
5 - 9
-
-
695836
5
-
30C, 24 h, 50% loss of activity
678989
5.5 - 10.1
-
-
679046
5.5 - 9
Cellulosimicrobium sp.
G3FBL1
1 h, more than 80% residual activity
714512
6 - 10
Q0IJR6
retains more than 75% of maximum activity after 1 h incubation
695697
6 - 9
D0UHB3
after incubation at 50C for 24 h
709829
6.5 - 10
B5BQ69
more than 80% of original activity after 12 h incubation at 4C
696843
7
B4XC07
inactivation above
697461
7.8
-
30C, 96 h, no loss of activity
678989
additional information
-
-
208795
additional information
-
-
208796
additional information
-
-
208800
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
stable up to
715233
38
E5RSM0
20 min, 50% residual activity, recombinant enzyme
714774
39
-
4 h, stable between pH 5 and 7
208798
40 - 70
Bispora sp.
B5LXD7
more than 65% of maximum activity within
695823
40
-
stable up to
208790
40
-
unstable above
656335
40
-
30 min, stable
680962
40
Q2LE69
stable below
680974
40
Q4WBS1
recombinant enzyme expressed in Aspergillus sojae
696916
40
Q5AZ53, Q5B7X2
3 h, 95% residual activity; 3 h, 95% residual activity
714350
45
B5BQ69
stable up to, for at least 20 min
696843
45
B4XC07
half-life less than 10 min
697461
45
B5LX62
30 min, 60% rsidual activity
707199
50
-
stable below
208788
50
-
stable below
208798
50
-
-
208804
50
Q0IJR6
60 min, 90% residual activity
695697
50
-
pH 6-9, 1 h, 70% residual activity
695836
50
Q4WBS1
recombinant enzyme expressed in Pichia pastoris
696916
50
Q49HI4
retains 90% of its activity after incubation for 60 min
699488
50
D0UHB3
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
709829
50
O05512
pH 6.0, stable for 30 min, incubation without substrate
714384
50
Cellulosimicrobium sp.
G3FBL1
half-life 15 min
714512
50
-
30 min, 20% residual activity
715233
52
-
20 min, 50% residual activity
714768
55
-
stable up to 55C
664167
55
-
15 min, almost complete loss of activity
678989
55
-
6 h, 50% residual activity
709495
60
-
for 1 h
208788
60
-
stable up to
208788
60
-
for 1 h
208809
60
Orpinomyces sp.
-
rapidly inactivated at 60C
664490
60
-
at pH 6.0, stable up to
679046
60
Q0PQY8
stable up to
679584
60
Q2LE69
half-life 50 min
680974
60
-
60 min, 90% residual activity
683011
60
-
6 h, 50% residual activity
695675
60
-
8 h, 50% residual activity
695675
60
Q0IJR6
20 min, complete loss of activity
695697
60
-
5 h, more than 50% residual activity
699365
60
Q49HI4
but no activity remains after incubation for 20 min
699488
60
B5LX62
30 min, complete loss of activity
707199
60
O05512
hlaf-life 4 min
714384
60
C6KL35
half-life 12 min
715882
65
-
stable up to
208795
65
-
completely stable at
208816
65
-
stable below
695836
70
-
stable up to
208785
70
-
-
208798
70
-
recombinant protein from Aspergillus oryzae
208807
70
P49425
1 h, 70% residual activity, truncated protein fragments produced in Escherichia coli, 1 h, 87% residual activity, protein derived from Rhodothermus marinus
654287
70
-
30 min, 20% residual activity
683011
70
Bispora sp.
B5LXD7
20 min, 50% residual activity
695823
70
-
stable for 30 min
707194
70
B6V876
half-life 56 h, pH 4.0
709828
75
-
30 min, 90% loss of activity
679046
80
-
no loss of activity over 16 h
208808
80
-
20 min, 18% residual activity, 30 min, complete loss of activity
683011
80
-
2 min, complete loss of activity
699365
90
P49425
1 h, 25% residual activity, truncated protein fragments produced in Escherichia coli
654287
90
-
half-life 15 min
714510
91
-
half-life 13 h
136061, 208813
additional information
-
-
208784, 208787
additional information
-
-
208788
additional information
-
-
208795
additional information
-
-
208796
additional information
-
-
208799, 208800
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is resistant to digestion by trypsin
Q0IJR6
enzyme is strongly resistant to pepsin and trypsin digestion
Bispora sp.
B5LXD7
enzyme is rather unstable and steadily loses activity during the purification process. Addition of 0.2% bovine serum albumine stabilizes
Q2I011
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
Penicillium wortmanni
-
may be used in preparations
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, stable for 18 h, pH 4-10
-
enzyme is stable at room temperature for at least 2 days
Q2LE69
cold
Fusicoccum sp.
-
-20C, a single freeze-thawing cycle results in loss of 80% of activity. Bovine serum albumine stabilizes
Q2I011
cold
-
-20C, MES buffer, 4 months, without loss of activity
-
4C, 48h, 20% residual activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both native protein and expressed in Saccharomyces cerevisiae
Q00012
recombinant protein expressed in Aspergillus oryzae
-
fast flow column chromatography
-
recombinant enzyme
B6V876
recombinant enzyme
D0UHB3
M-I, M-II, M-III
-
four enzyme forms
-
from culture supernatant
-
recombinant enzyme
B5LX62
recombinant protein containing active protein domain
-
from digestive fluid
-
purification from seedling
Q2I011
recombinant protein
-
cation exchange chromatography
Q8L5J1
salt extraction, dialysis, cation exchange chromatography
-
recombinant protein expressed in Escherichia coli
-
recombinant enzyme
Q8P9S0
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli
E5RSM0
expression in Aspergillus niger
-
expression in Aspergillus oryzae
-
expression in Yarrowia lipolytica
-
expression in Aspergillus sojae and Pichia pastoris
Q4WBS1
expression in Pichia pastoris; expression in Pichia pastoris
Q5AZ53, Q5B7X2
expression in Pichia pastoris
-
expression in Pichia pastoris
Q2LE69
expression in Escherichia coli
Q49HI4
expression in Pichia pastoris and Escherichia coli
Q0IJR6
expression in Escherichia coli
D0UHB3
expression in Escherichia coli
-
expression in Pichia pastoris
B5LX62
expression in Escherichia coli
Bispora sp.
B5LXD7
-
Caldicellulosiruptor sp.
-
expressed in Escherichia coli
-
expression in Escherichia coli
Cellulosimicrobium sp.
G3FBL1
expression in Escherichia coli
-
both ManA and ManB
-
exprression in Escherichia coli fused with thioredoxin gene
B4XC07
expression in Escherichia coli
-
expressed in Pichia pastoris
-
expressed in Saccharomyces cerevisiae and Escherichia coli
Orpinomyces sp.
-
expression in Escherichia coli
-
expression in Aspergillus niger
Q0PQY8
expressed in Arabidopsis thaliana transformed with Agrobacterium tumefaciens
Q6YM50
expressed in Escherichia coli
-
expressed in Escherichia coli strain BL21
Q8L5J1
expression in Escherichia coli
A5IMX7
expression in Escherichia coli
-
expression in Escherichia coli
Q8P9S0
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression upon seed imbibition
-
isoform manA transcription is positively regulated by Clp and RpfF and induced by locust bean gum
Q8P9S0
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S289W
Q5AZ53, Q5B7X2
mutation lowers KM for mannooligosaccharides by 30-45% and increases transglycosylation yield by 50% compared to wild-type
W283S
Q5AZ53, Q5B7X2
mutation in subsite +1, mutation results in increase in KM value, reduction in the transglycosylation yield by 30-45% and decrease in activity towards mannans
S289W
-
mutation lowers KM for mannooligosaccharides by 30-45% and increases transglycosylation yield by 50% compared to wild-type
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E167A
Q5PSP8
about 60% loss of catalytic efficiency
E266A
Q5PSP8
complete loss of activity
D283A
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increase of Km-value by about 80%
D283H
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dramatic decrease of Km-value
E212A
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dramatic decrease of Km-value
H143A
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decrease of Km-value by about 50%
H211A
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decrease of Km-value by about 30%
H211N
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dramatic decrease of Km-value
H211N/D283H
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decrease of Km-value by about 50%
W156A
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increase of Km-valueby almost 80%
W162A
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increase of Km-value by about 50%
W217A
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increase of Km-value by more than 100%
Y285A
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dramatic decrease of Km-value
E222A
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no catalytic acitivity
W283S
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mutation in subsite +1, mutation results in increase in KM value, reduction in the transglycosylation yield by 30-45% and decrease in activity towards mannans
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additional information
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gene optimization according to the codon usage bias in Pichia pastoris and synthesis by splicing overlap extension PCR
additional information
-
gene optimization according to the codon usage bias in Pichia pastoris and synthesis by splicing overlap extension PCR
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H1A/H23A
Q5PSP8
about 10% loss of catalytic efficiency
additional information
B5LX62
optimization of mannanase gene for expression in Pichia pastoris by substitution of 258 nucleotides with their corresponding counterparts according to the codon usage in Pichia pastoris, which has no change on the beta-mannanase amino acid sequence
additional information
Bacillus subtilis MA139
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optimization of mannanase gene for expression in Pichia pastoris by substitution of 258 nucleotides with their corresponding counterparts according to the codon usage in Pichia pastoris, which has no change on the beta-mannanase amino acid sequence
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E91A
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no catalytic acitivity
additional information
C6KL35
deletion of the CBM6 domain increases the enzyme stability while enabling it to retain 80% and 60% of its initial activity after treatment at 80C and 90C for 30 min
additional information
-
deletion of the CBM6 domain increases the enzyme stability while enabling it to retain 80% and 60% of its initial activity after treatment at 80C and 90C for 30 min
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additional information
-
the cultivar Walter displays an inactive enzyme due to the absence of the C-terminal four amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein
additional information
Q8P9S0
mutant MG17 is catalytically inactive, mutant protein is present at wild-type molecular mass
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
can be completely renatured after denaturation in 6 M guanidine hydrochloride
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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production of enzyme by expression in Aspergillus niger under control of the Aspergillus niger glyceraldehyde-3-phosphate dehydrogenase promoter gpdP and the Aspergillus awamori glucoamylase terminator glaAT. The glucose concentration and the organic nitrogen source have an effect on both the volumetric enzyme activity and the specific enzyme activity. The highest mannanase activity levels of 16596 nkat ml-1 and 574 nkat mg-1 dcw are obtained for Aspergillus niger when cultivated in a process-viable medium containing corn steep liquor as the organic nitrogen source and high glucose concentrations
synthesis
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expression in Yarrowia lipolytica using beta-mannosidase's own secretion signal. Fed batch fermentations result in a 3.9fold increase in volumetric enzyme activity compared with batch fermentation, and a maximum titre of 26,139 nkat/ml
synthesis
Aspergillus aculeatus MRC11624
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production of enzyme by expression in Aspergillus niger under control of the Aspergillus niger glyceraldehyde-3-phosphate dehydrogenase promoter gpdP and the Aspergillus awamori glucoamylase terminator glaAT. The glucose concentration and the organic nitrogen source have an effect on both the volumetric enzyme activity and the specific enzyme activity. The highest mannanase activity levels of 16596 nkat ml-1 and 574 nkat mg-1 dcw are obtained for Aspergillus niger when cultivated in a process-viable medium containing corn steep liquor as the organic nitrogen source and high glucose concentrations
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nutrition
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pulp production
pharmacology
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tailoring of hydrogel release profiles of potential interest for intestine drug delivery. The rate of hydrolysis of O-acetyl-galactomannan hydrogels modified with alpha-galactosidase increases with decreasing degree of substitution. The addition of alpha-mannanase significantly enhances the release of bovine serum albumin encapsulated in hydrogels with a degree of substitution of 0.36, reaching a maximum of 95% released bovine serum albumin after eight hours compared to 60% without enzyme
synthesis
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production of beta-mannanase using palm kernel cake as substrate in solid substrate fermentation. Optimal conditions are incubation temperature of 32C, initial moisture level of 59% and aeration rate of 0.5 l/min, resulting in a beta-mannanase yield of 2231.26 U/g
synthesis
-
development of a fed-batch strategy for engineered enzyme, using high cell-density fermentation. Mannanase activity reaches 5069 U/ml after cultivation for 56 h in 50 l fermenter
synthesis
-
production of beta-mannanase from palm kernel cake as a substrate in solid substrate fermentation. A statistical model suggests that the optimal conditions for attaining the highest level of beta-mannanase are incubation temperature of 32C, initial moisture level of 59% and aeration rate of 0.5 l/min. A beta-mannanase yield of 2231.26 U/g is obtained under these optimal conditions
synthesis
-
development of a fed-batch strategy for engineered enzyme, using high cell-density fermentation. Mannanase activity reaches 5069 U/ml after cultivation for 56 h in 50 l fermenter
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synthesis
Aspergillus niger FTCC
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production of beta-mannanase using palm kernel cake as substrate in solid substrate fermentation. Optimal conditions are incubation temperature of 32C, initial moisture level of 59% and aeration rate of 0.5 l/min, resulting in a beta-mannanase yield of 2231.26 U/g, production of beta-mannanase from palm kernel cake as a substrate in solid substrate fermentation. A statistical model suggests that the optimal conditions for attaining the highest level of beta-mannanase are incubation temperature of 32C, initial moisture level of 59% and aeration rate of 0.5 l/min. A beta-mannanase yield of 2231.26 U/g is obtained under these optimal conditions
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synthesis
Aspergillus niger FTCC 5003
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production of beta-mannanase using palm kernel cake as substrate in solid substrate fermentation. Optimal conditions are incubation temperature of 32C, initial moisture level of 59% and aeration rate of 0.5 l/min, resulting in a beta-mannanase yield of 2231.26 U/g, production of beta-mannanase from palm kernel cake as a substrate in solid substrate fermentation. A statistical model suggests that the optimal conditions for attaining the highest level of beta-mannanase are incubation temperature of 32C, initial moisture level of 59% and aeration rate of 0.5 l/min. A beta-mannanase yield of 2231.26 U/g is obtained under these optimal conditions
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agriculture
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10 U/mg enzyme can hydrolyze more than 90% of 10 mg/ml konjac flour at 50C in 24 h
agriculture
Bacillus sp. MSK-5
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10 U/mg enzyme can hydrolyze more than 90% of 10 mg/ml konjac flour at 50C in 24 h
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biotechnology
B5LX62
optimization of mannanase gene for expression in Pichia pastoris by substitution of 258 nucleotides with their corresponding counterparts according to the codon usage in Pichia pastoris, which has no change on the beta-mannanase amino acid sequence. Compared to the activity of wild-type, the expression enzyme of the optimized beta-mannanase gene acquires approximately 35% more activity
synthesis
O05512
expression in Escherichia coli based on T7 RNA polymerase promoter and tac promoter systems. Both Escherichia coli OmpA signal peptide and native Bacillus signal peptide can be used efficiently for secretion of recombinant protein. Enzyme can be harvested from whole cell lysate, periplasmic extract or culture broth 4-20 h after induction by IPTG
biotechnology
Bacillus subtilis MA139
-
optimization of mannanase gene for expression in Pichia pastoris by substitution of 258 nucleotides with their corresponding counterparts according to the codon usage in Pichia pastoris, which has no change on the beta-mannanase amino acid sequence. Compared to the activity of wild-type, the expression enzyme of the optimized beta-mannanase gene acquires approximately 35% more activity
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degradation
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when assembled with the mini-CbpA, which contains a carbohydrate-binding module that provides proximity to insoluble substrates, a mixture of endoglucanase E and ManB at a molar ratio of 1:2 shows the highest synergistic effect of 2.4fold on locust bean gum degradation. The mixture at a ratio of 1:3 shows the highest synergistic effect of 2.8fold on guar gum
paper production
Q8WPJ2
cellulose degradation
industry
Q0PQY8
when used to treat softwood pulp, enzyme hydrolyzes mainly glucomannan and exhibits a positive effect as a prebleaching agent
agriculture
Q8L5J1
fruit ripening and seed germination
agriculture
-
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
biotechnology
Q8L5J1
bio-bleaching for kraft pulp production