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4-nitrophenyl-maltopentaoside + H2O
4-nitrophenol + maltopentaose
-
-
-
-
?
amylopectin + H2O
maltotetraose + ?
amylose + H2O
maltotetraose
amylose + H2O
maltotetraose + ?
-
enzyme hydrolysates of amylose contains a considerably lower concentration of reducing sugars
-
-
?
azurine cross-linked amylose + H2O
maltotetraose + ?
-
-
-
-
?
glycogen + H2O
maltotetraose
maize starch + H2O
maltotetraose + ?
-
the enzyme decreases the end viscosity of the maize starch suspension
-
-
?
maltoheptaose + H2O
maltotetraose + maltotriose
maltohexaose + H2O
maltotetraose + maltose
oyster glycogen + H2O
maltotetraose + ?
starch + H2O
maltotetraose
starch + H2O
maltotetraose + ?
-
the enzyme is capable of producing more than 45% maltotetraose from liquefied starch under optimal conditions
-
-
?
additional information
?
-
amylopectin + H2O
maltotetraose + ?
-
-
-
-
?
amylopectin + H2O
maltotetraose + ?
-
-
-
?
amylopectin + H2O
maltotetraose + ?
-
-
-
?
amylopectin + H2O
maltotetraose + ?
-
-
-
-
?
amylopectin + H2O
maltotetraose + ?
-
recombinant and native enzyme
-
?
amylopectin + H2O
maltotetraose + ?
-
-
-
?
amylopectin + H2O
maltotetraose + ?
-
-
-
-
?
amylopectin + H2O
maltotetraose + ?
-
-
-
-
?
amylopectin + H2O
maltotetraose + ?
-
-
-
-
?
amylose + H2O
maltotetraose
-
-
-
-
?
amylose + H2O
maltotetraose
-
-
-
-
?
amylose + H2O
maltotetraose
-
-
-
?
amylose + H2O
maltotetraose
-
-
-
?
amylose + H2O
maltotetraose
-
recombinant and native enzyme
-
-
?
amylose + H2O
maltotetraose
-
-
-
?
amylose + H2O
maltotetraose
-
-
-
?
glycogen + H2O
maltotetraose
-
-
-
-
?
glycogen + H2O
maltotetraose
-
-
-
-
?
glycogen + H2O
maltotetraose
-
recombinant and native enzyme, oyster and rabbit liver glycogen
-
-
?
glycogen + H2O
maltotetraose
-
-
-
-
?
glycogen + H2O
maltotetraose
-
oyster and shellfish glycogen
-
?
glycogen + H2O
maltotetraose
-
-
-
-
?
glycogen + H2O
maltotetraose
-
oyster and shellfish glycogen
-
?
maltoheptaose + H2O
maltotetraose + maltotriose
-
-
-
-
?
maltoheptaose + H2O
maltotetraose + maltotriose
-
-
-
?
maltohexaose + H2O
maltotetraose + maltose
-
-
-
-
?
maltohexaose + H2O
maltotetraose + maltose
-
-
-
-
?
maltohexaose + H2O
maltotetraose + maltose
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
oyster glycogen + H2O
maltotetraose + ?
-
-
-
-
?
oyster glycogen + H2O
maltotetraose + ?
-
-
-
-
?
starch + H2O
maltotetraose
-
-
-
?
starch + H2O
maltotetraose
-
-
-
?
starch + H2O
maltotetraose
-
-
-
?
starch + H2O
maltotetraose
-
-
-
?
starch + H2O
maltotetraose
-
-
-
-
?
starch + H2O
maltotetraose
-
recombinant and native enzyme
-
?
starch + H2O
maltotetraose
-
-
-
-
?
starch + H2O
maltotetraose
-
-
-
?
starch + H2O
maltotetraose
-
amylase A and B potato starch
-
?
starch + H2O
maltotetraose
-
-
-
?
starch + H2O
maltotetraose
-
amylase A and B potato starch
-
?
starch + H2O
maltotetraose
-
-
-
?
starch + H2O
maltotetraose
-
-
-
?
starch + H2O
maltotetraose
-
-
-
-
?
starch + H2O
maltotetraose
-
-
-
?
starch + H2O
maltotetraose
-
-
-
?
starch + H2O
maltotetraose
-
-
-
-
?
starch + H2O
maltotetraose
-
-
-
?
starch + H2O
maltotetraose
-
-
-
?
starch + H2O
maltotetraose
-
-
-
?
additional information
?
-
-
five alkaline amylases are produced in culture broth
-
-
?
additional information
?
-
-
five alkaline amylases are produced in culture broth
-
-
?
additional information
?
-
-
the enzyme has a low degree of multiple attack, enzyme action pattern, overview
-
-
?
additional information
?
-
-
constitutive maltotetraose-producing amylase using glycose as carbon source
-
-
?
additional information
?
-
-
more amylase production under high hydrostatic pressure than under atmospheric pressure
-
-
?
additional information
?
-
-
constitutive maltotetraose-producing amylase using glycose as carbon source
-
-
?
additional information
?
-
-
more amylase production under high hydrostatic pressure than under atmospheric pressure
-
-
?
additional information
?
-
-
maltotriose-forming exo-amylase, enzyme exists in two forms: the 57 kDa G4-1 with a raw starch binding domain and the 46 kDa G4-2, which is a spontaneous hydrolysis product of G4-1 lacking the raw starch binding domain, domain structure
-
-
?
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Ag+
-
AgNO3, recombinant and native enzyme
Al3+
-
F1 and F2 form 30% inhibition
Co2+
-
F1 and F2 form 47% inhibition
EDTA
-
1 mM, 82% inhibition
Fe2+
-
F1 form, 96% F2 form, 98% inhibition
N-bromosuccinimide
-
F1 form, pH 6.5 complete inhibition, pH 8.0, 93% inhibition, F2 form, pH 6.5, 95% inhibition, pH 8.0, 28% inhibition
Ni2+
-
F1 form 62%, F2 form 67% inhibition
Pb2+
-
Pb(OAc)2, recombinant and native enzyme
phenylmethylsulfonyl fluoride
-
1 mM, 4°C, 10 h incubation, 76% inhibition
Cu2+
-
-
Cu2+
-
CuSO4, recombinant and native enzyme
Cu2+
-
1 mM CuCl2, amylase A, 98% inhibition, amylase B, complete inhibition
Cu2+
-
F1 and F2 form 92% inhibition
Fe3+
-
FeCl3, recombinant and native enzyme
Fe3+
-
1 mM FeCl3, amylase A, 73% inhibition, amylase B, 87% inhibition
Fe3+
-
F1 form, 75% F2 form, 76% inhibition
Hg2+
-
1 mM HgCl2, complete inhibition
Hg2+
-
1 mM HgCl2, amylase A, 99% inhibition, amylase B, 97% inhibition
Hg2+
-
F1 and F2 form, complete inhibition
Zn2+
-
-
Zn2+
-
1 mM ZnCl2, amylase A 99% inhibition, amylase B, 97% inhibition
Zn2+
-
F1 form 94%, F2 form 96% inhibition
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50
-
G4-1-form heat-sensitive than G4-2 form
55
-
F1 and F2 form, complete loss of activity in the absence of Ca2+
70
-
pH 6.0, 30 min, 80% activity remaining
80
-
pH 6.0, 30 min, 30% activity remaining
90
-
pH 6.0, 30 min, inactivation
40
-
unstable below
40
-
recombinant and native enzyme stable on heating in 10 mM acetate buffer, pH 6.0, 30 min, 40°C and below
40
-
pH 6.0, 30 min, completely stable up to
40
-
amylase A and B, pH 7, full activity below
40
-
F1 and F2 form, stable below on the treatment at pH 8.0, 60 min in the presence or absence of 5 mM CaCl2
60
-
1 mM CaCl2 and 1% soluble starch enhance thermostability
60
-
recombinant and native enzyme, complete loss of activity
60
-
10 min, amylase A and B, inactivation
60
-
F1 and F2 form, complete loss of activity in the presence of Ca2+
additional information
-
Ca2+ protects enzyme from heat
additional information
-
2 mM CaCl2, thermal stability of the recombinant and native enzymes increase
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Robyt, J.F.; Ackerman, R.J.
Isolation, purification, and characterization of a maltotetraose-producing amylase from Pseudomonas stutzeri
Arch. Biochem. Biophys.
145
105-114
1971
Pseudomonas stutzeri
brenda
Dellweg, H.; John, M.; Schmidt, J.
Amylases from Pseudomonas stutzeri. Affinity chromatography of exo-maltotetraohydrolase using Sephadex G-100 as an adsorbent
Eur. J. Appl. Microbiol. Biotechnol.
1
191-198
1975
Pseudomonas stutzeri, Pseudomonas stutzeri NRRL B-3389
-
brenda
Sakano, Y.; Kashiyama, E.; Kobayashi, T.
Purification of alpha-maltotetraose-forming exo-amylase of Pseudomonas stutzeri-two forms of the amylase and their enzymatic properties
Agric. Biol. Chem.
47
1761-1768
1983
Pseudomonas stutzeri, Pseudomonas stutzeri NRRL B-3389
-
brenda
Kimura, T.; Ogata, M.; Yoshida, M.; Nakakuki, T.
Continuous production of maltotetraose using immobilized Pseudomonas stutzeri
Biotechnol. Bioeng.
32
669-676
1988
Pseudomonas stutzeri
brenda
Kimura, T.; Ogata, M.; Yoshida, M.; Nakakuki, T.
Stability of immobilized maltotetraose-forming amylase from Pseudomonas stutzeri
Biotechnol. Bioeng.
33
845-855
1989
Pseudomonas stutzeri
brenda
Zhou, J.; Takano, T.; Kobayashi, S.
Cloning of exo-maltotetrahydrolase gene from Pseudomonas saccharophila in Escherichia coli
Agric. Biol. Chem.
53
301-302
1989
Pelomonas saccharophila, Pelomonas saccharophila IAM 1504
-
brenda
Nakada, T.; Kubota, M.; Sakai, S.; Tsujisaka, Y.
Purification and characterization of two forms of maltotetraose-forming amylase from Pseudomonas stutzeri
Agric. Biol. Chem.
54
737-743
1990
Pseudomonas stutzeri, Pseudomonas stutzeri MO-19
brenda
Takasaki, Y.; Shinohara, H.; Tsuruhisa, M.; Hayashi, S.; Imada, K.
Maltotetraose-producing amylase from Bacillus sp. MG-4
Agric. Biol. Chem.
55
1715-1720
1991
Niallia circulans, Niallia circulans MG-4
-
brenda
Zhou, J.; Baba, T.; Takano, T.; Kobayashi, S.; Arai, Y.
Properties of the enzyme expressed by the Pseudomonas saccharophila maltotetrahydrolase gene (mta) in Escherichia coli
Carbohydr. Res.
223
255-261
1992
Pelomonas saccharophila
brenda
Fogarty, W.M.; Bourke, A.C.; Kelly, C.T.; Doyle, E.M.
A constitutive maltotetraose-producing amylase from Pseudomonas sp. IMD 353
Appl. Microbiol. Biotechnol.
42
198-203
1994
Pseudomonas sp., Pseudomonas sp. IMD 353
-
brenda
Woo, G.J.; McCord, J.D.
Bioconversion of starches into maltotetraose using Pseudomonas stutzeri maltotetraohydrolase in a membrane recycle bioreactor: effect of multiple enzyme systems and mass balance study
Enzyme Microb. Technol.
16
1016-1020
1994
Pseudomonas stutzeri, Pseudomonas stutzeri NRRL B-3389
-
brenda
Kim, T.U.; Gu, B.G.; Jeong, J.Y.; Byun, S.M.; Shin, Y.C.
Purification and characterization of a maltotetraose-forming alkaline alpha-amylase from an alkalophilic Bacillus strain, GM8901
Appl. Environ. Microbiol.
61
3105-3112
1995
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) GM8901
brenda
Kobayashi, S.; Takaki, Y.; Kobata, K.; Takami, H.; Inoue, A.
Characterization of maltotetraohydrolase produced Pseudomonas sp. MS300 isolated from the deepest site of the Mariana Trench
Extremophiles
2
401-407
1998
Pseudomonas sp., Pseudomonas sp. MS300
brenda
Yoshioka, Y.; Hasegawa, K.; Matsuura, Y.; Katsube, Y.; Kubota, M.
Crystal structures of a mutant maltotetraose-forming exo-amylase cocrystallized with maltopentaose
J. Mol. Biol.
271
619-628
1997
Pseudomonas stutzeri
brenda
Morishita, Y.; Hasegawa, K.; Matsuura, Y.; Katsube, Y.; Kubota, M.; Sakai, S.
Crystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri
J. Mol. Biol.
267
661-672
1997
Pseudomonas stutzeri
brenda
Mezaki, Y.; Katsuya, Y.; Kubota, M.; Matsuura, Y.
Crystallization and structural analysis of intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri
Biosci. Biotechnol. Biochem.
65
222-225
2001
Pseudomonas stutzeri
brenda
Derde, L.J.; Gomand, S.V.; Courtin, C.M.; Delcour, J.A.
Characterisation of three starch degrading enzymes: thermostable beta-amylase, maltotetraogenic and maltogenic alpha-amylases
Food Chem.
135
713-721
2012
Pelomonas saccharophila
brenda
Bae, W.; Lee, S.H.; Yoo, S.H.; Lee, S.
Utilization of a maltotetraose-producing amylase as a whole wheat bread improver: dough rheology and baking performance
J. Food Sci.
79
E1535-E1540
2014
Bacillus licheniformis
brenda