3.2.1.2: beta-amylase
This is an abbreviated version!
For detailed information about beta-amylase, go to the full flat file.
Word Map on EC 3.2.1.2
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3.2.1.2
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starch
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alpha-amylase
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maltose
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barley
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potato
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soybean
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sweet
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amylopectin
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amylolytic
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glucoamylase
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endosperm
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hordeum
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amylases
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pullulanase
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debranching
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dextrin
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nutrition
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maltotetraose
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thermosulfurogenes
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isoamylase
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beta-limit
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starch-degrading
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amyloglucosidase
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polymyxa
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maltotriose
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maltopentaose
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granule-bound
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alpha-cyclodextrin
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extrachloroplastic
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industry
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sporamin
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molecular biology
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brewing
- 3.2.1.2
- starch
- alpha-amylase
- maltose
- barley
- potato
- soybean
-
sweet
- amylopectin
-
amylolytic
- glucoamylase
- endosperm
- hordeum
- amylases
- pullulanase
-
debranching
- dextrin
- nutrition
- maltotetraose
- thermosulfurogenes
- isoamylase
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beta-limit
-
starch-degrading
- amyloglucosidase
- polymyxa
- maltotriose
- maltopentaose
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granule-bound
- alpha-cyclodextrin
-
extrachloroplastic
- industry
-
sporamin
- molecular biology
- brewing
Reaction
Synonyms
(1-4)-alpha-D-glucan maltohydrolase, 1,4-alpha-D-glucan malto-hydrolase, 1,4-alpha-D-glucan maltohydrolase, 1-4-alpha-glucan maltohydrolase, alpha-1,4-glucan maltohydrolase, amylase, beta-, ARATH, BAM-1, BAM-2, BAM-3, BAM-5, BAM-6, BAM-7, BAM-8, BAM-9, BAM1, BAM3, BAM4, BCB, beta amylase, beta-amylase, beta-amylase 1, beta-amylase I, beta-amylase1, beta-amylase2, beta-amylase8, BMY, Bmy1, Bmy2, Cs-COR018, CT-BMY, glycogenase, More, PF0870, saccharogen amylase, saccharogenamylase, SBA, Sd1, Sd2H, Sd2L, spoII, TCMA, TR-BAMY, type I beta-amylase, type II beta-amylase
ECTree
3.2.1.2 beta-amylaseAdvanced search results
results (
results (Temperature Stability
Temperature Stability on EC 3.2.1.2 - beta-amylase
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TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
100
2 h, 22% loss of activity. Ater 4 h of incubation, the relative activity of the enzyme is 45%
40
50
55
57
57.5
60
65
69
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30 min, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S, 50% inactivation
70
80
85
the half-life is 69 min, 225 min, and 255 min at pH 5.0, pH 6.0, and pH 7.0
90
additional information
50
2 h, purified enzyme retains 100 % relative activity. Ater 4 h of incubation, the relative activity of the enzyme is 80%
57.5
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30 min, analysis of isozyme thermostability of different species and subspecies, overview
57.5
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30 min, analysis of isozyme thermostability of different cultivars, overview
60
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pH 5.4, 90 min, 38% loss of activity of isoenzyme 2, 55% loss of activity of isoenzyme 6
60
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pH 4.8, half-life: 291 min for the first decay segment, 1790 min for the second decay segment
60
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30 min: 65% loss of activity, 60 min: 75% loss of activity, 90 min: 100% loss of activity
60
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temperature optimum, but enzyme loses activity when exposed to 60°C, irreversible thermodenaturation, thermodenaturation kinetics, Mn2+ and exogenous thiols like dithiothreitol, 2-mercaptoethanol or cysteine HCl play a remarkable role in reactivation of thermally denatured enzyme
60
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the thermoinactivated enzyme (exposed to 60°C for 10 min) could be partially reactivated by the addition of 1 mM 2-mercaptoethanol (7.3% increase) and 4 mM Mn2+ (14% increase)
60
2 h, purified enzyme retains 100 % relative activity. Ater 4 h of incubation, the relative activity of the enzyme is 80%
70
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pH 4.8, half-life: 14.4 min for the first decay segment, 37.9 min for the second decay segment
70
2 h, purified enzyme retains 100 % relative activity. Ater 4 h of incubation, the relative activity of the enzyme is 72%
80
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unstable in absence of substrate or Ca2+, stable in presence of 5 mM Ca2+ or 1% substrate
80
2 h, purified enzyme retains 100 % relative activity. Ater 4 h of incubation, the relative activity of the enzyme is 63%
90
2 h, 15% loss of activity. Ater 4 h of incubation, the relative activity of the enzyme is 54%
additional information
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the 3 allelic forms of beta-amylase Sd1, Sd2H and Sd2L exhibit different thermostability, due to two amino acid substitutions, V233A and L347S, which increase the thermostability index T50 of Sd2L by 1.9°C and 2.1°C, respectively
additional information
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the recombinant isozyme Bmy2 from cultivar Morex shows a slightly higher thermostability compared to the recombinant enzyme from cultivar Steptoe, T50 values, residues D238, M337, and Q362 are involved in the Morex Bmy2 thermostability, overview
additional information
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thermal inactivation kinetics of the enzyme at different pressure/temperature conditions, mechanism, overview
additional information
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immobilization of both native and modified enzymes on a amino silica results in thermostabilization of the enzyme
additional information
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increased thermoresistance of beta-amylase is achieved through stabilization of thiol groups present at the active site by manipulating the enzymes environment by the addition of Mn2+ and 2-mercaptoethanol, and through immobilization. Both of which would increase the enzymes practical importance and industrial utility
additional information
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stability is greatly enhanced by addition of 5 mM CaCl2
