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0.01 - 0.281
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
additional information
starch
0.01
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, kcat/Km: L134R/S320A, 680000 1/s/M, 25°C, pH 6.0
0.0113
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 740000 1/s/M, 25°C, pH 6.0
0.0117
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 710000 1/s/M, 25°C, pH 6.0
0.012
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 770000 1/s/M, 25°C, pH 6.0
0.137
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, L134R/S320A, kcat/Km: L134R/S320A, 1910000 1/s/M, 37°C, pH 4.5
0.147
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 1420000 1/s/M, 37°C, pH 6.5
0.171
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 1350000 1/s/M, 37°C, pH 4.5
0.185
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, L134R/S320A, kcat/Km: L134R/S320A, 680000 1/s/M, 37°C, pH 5.5
0.186
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 1210000 1/s/M, 37°C, pH 4.5
0.19
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, L134R/S320A, kcat/Km: L134R/S320A, 1100000 1/s/M, 37°C, pH 6.5
0.193
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 1070000 1/s/M, 37°C, pH 5.5
0.2
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 1230000 1/s/M, 37°C, pH 5.5
0.201
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 920000 1/s/M, 37°C, pH 6.5
0.201
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 870000 1/s/M, 37°C, pH 5.5
0.205
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 880000 1/s/M, 37°C, pH 6.5
0.281
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 140000 1/s/M, 37°C, pH 4.5
additional information
starch
0.60 mg/ml, double mutant, kcat/Km: 1560 ml/mg/s, L134R/S320A, 25°C, pH 6.0
additional information
starch
-
0.60 mg/ml, double mutant, kcat/Km: 1560 ml/mg/s, L134R/S320A, 25°C, pH 6.0
additional information
starch
0.61 mg/ml, mutant S329A, kcat/Km: 1870 ml/mg/s, 25°C, pH 6.0
additional information
starch
-
0.61 mg/ml, mutant S329A, kcat/Km: 1870 ml/mg/s, 25°C, pH 6.0
additional information
starch
0.64 mg/ml, mutant L134R, kcat/Km: 1670 ml/mg/s, 25°C, pH 6.0
additional information
starch
-
0.64 mg/ml, mutant L134R, kcat/Km: 1670 ml/mg/s, 25°C, pH 6.0
additional information
starch
0.86 mg/ml, wild-type, kcat/Km: 1920 ml/mg/s, 25°C, pH 6.0
additional information
starch
-
0.86 mg/ml, wild-type, kcat/Km: 1920 ml/mg/s, 25°C, pH 6.0
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
detailed kinetic analysis
-
additional information
additional information
-
thermodynamics and kinetics
-
additional information
additional information
-
KM for soluble starch is constant at pH 5.0-7.0 and increases greatly with decreasing pH from 5.0 to 2.8 and slightly with increasing pH from 7.5 to 9.2, alpha-amylase PA
-
additional information
additional information
Lineweaver-Burk kinetics, Km for raw starch from jackfruit is 5.56 mg/ml
-
additional information
additional information
-
Lineweaver-Burk kinetics, Km for raw starch from jackfruit is 5.56 mg/ml
-
additional information
potato starch
-
free enzyme, Km: 0.4 mg/ml, Vmax: 25 mg starch degraded/ml/min/mg protein, immobilized enzyme, first use, Km: 0.98 mg/ml, Vmax: 23.3 mg starch degraded/ml/min/mg protein, first reuse, Km: 1.75 mg/ml, Vmax: 10.4 mg starch degraded/ml/min/mg protein. The higher Km value and the lower affinity for the substrate caused by diffiusional limitations and steric effects leading to a decrease in the accessibility of substrate to the enzyme active site
-
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7.86 - 266
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
additional information
starch
7.86
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, L134R/S320A, kcat/Km: L134R/S320A, 680000 1/s/M, 25°C, pH 6.0
8.14
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 710000 1/s/M, 25°C, pH 6.0
8.32
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 740000 1/s/M, 25°C, pH 6.0
8.73
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 770000 1/s/M, 25°C, pH 6.0
34
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 140000 1/s/M, 37°C, pH 4.5
175
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 880000 1/s/M, 37°C, pH 6.5
175
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 870000 1/s/M, 37°C, pH 5.5
186
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 920000 1/s/M, 37°C, pH 6.5
187
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 1230000 1/s/M, 37°C, pH 5.5
201
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 1070000 1/s/M, 37°C, pH 5.5
205
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
wild-type, kcat/Km: 1420000 1/s/M, 37°C, pH 6.5
209
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, L134R/S320A, kcat/Km: L134R/S320A, 1100000 1/s/M, 37°C, pH 6.5
219
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant S329A, kcat/Km: 1210000 1/s/M, 37°C, pH 4.5
233
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, L134R/S320A, kcat/Km: L134R/S320A, 680000 1/s/M, 37°C, pH 5.5
234
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
mutant L134R, kcat/Km: 1350000 1/s/M, 37°C, pH 4.5
266
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
double mutant, L134R/S320A, kcat/Km: L134R/S320A, 1910000 1/s/M, 37°C, pH 4.5
additional information
starch
double mutant, L134R/S320A, kcat/Km: 1560 ml/mg/s, L134R/S320A, 25°C, pH 6.0
additional information
starch
-
double mutant, L134R/S320A, kcat/Km: 1560 ml/mg/s, L134R/S320A, 25°C, pH 6.0
additional information
starch
mutant L134R, kcat/Km: 1670 ml/mg/s, 25°C, pH 6.0
additional information
starch
-
mutant L134R, kcat/Km: 1670 ml/mg/s, 25°C, pH 6.0
additional information
starch
mutant S329A, kcat/Km: 1870 ml/mg/s, 25°C, pH 6.0
additional information
starch
-
mutant S329A, kcat/Km: 1870 ml/mg/s, 25°C, pH 6.0
additional information
starch
wild-type, kcat/Km: 1920 ml/mg/s, 25°C, pH 6.0
additional information
starch
-
wild-type, kcat/Km: 1920 ml/mg/s, 25°C, pH 6.0
additional information
additional information
-
-
-
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100
around 60% of the enzyme activity is still detectable in wild-type and mutant enzymes after incubating in a boiling bath for 60 min
70
30 min, whole cells, the amylase activity is completely stable
80
30 min, whole cells, 90% amylase activity is remaining
90
approx. 25% loss of activity after 150 min, approx. 60% loss of activity after 400 min
110
-
1 h, 50-60% loss of activity
20 - 70
-
purified native enzyme, 10 min, completely stable at
41
-
T50-value at pH 4.5, without CaCl2, alpha-amylase PA
60 - 70
recombinant enzyme, stable up to in absence of Ca2+
63
-
T50-value at pH 4.5, 5 mM CaCl2, alpha-amylase PA
71
-
T50-value at pH 6.0, without CaCl2, alpha-amylase PA
78
-
half-life of the mosaic hybrid enzymes ALA76-151, ALA17-151: 5 min
84
-
T50-value at pH 6.0, 5 mM CaCl2, alpha-amylase PA
85
-
60 min, with the exception of the enzyme from strain NCIB 9668, more than 98% of the activity is retained
100
-
4 h, in presence of starch, completely stable
100
-
remains active to 2 h in presence of substrate
100
-
purified native enzyme, 10 min, no activity remaining
60
-
5 min, stable
60
-
3 h, in absence of substrate, 9% loss of activity
70
-
-
70
-
3 h, in absence of substrate, 21% loss of activity
75
-
-
80
-
-
80
-
5 min, 55% loss of activity
80
-
90 min, in absence of substrate, 29% loss of activity
80
-
30% loss of activity in the absence of additive, 21%, 5%, 7% and 10% loss of activity in the presence of 20% trehalose, sorbitol, mannitol and glycerol, respectively
80
-
purified native enzyme, 10 min, 70% activity remaining
80
recombinant enzyme, stable up to in presence of Ca2+
90
-
-
90
-
30 min, 10-20% loss of activity of the hybrid enzymes AL76, AL108, and AL112, 35-50% loss of activity of the hybrid enzymes AL142, AL147, AL149, AL151, LAL19-163, AL163, and AL174. About 90% of activity after 30 min of the hybrid enzymes AL231, AL256 and AL263
90
-
half-life of hybrid enzymes: about 50 min for LA431, AL17, Al34
90
-
no loss of activity in the presence of 50% toluene or n-octane
90
-
pH 5.5, 1 h, 50% inactivation, alpha-amylase PA
90
-
purified native enzyme, 10 min, 10% activity remaining
95
-
approx. 50% loss of activity after 15 min, approx. 80% loss of activity after 15 min
95
-
covalent binding of thermostable alpha-amylase on calcium alginate provides a 80% activity based on the immobilized protein for the first cycle and hydrolyzes a total of 51 mg starch/s/mg protein after seven cycles at 95°C
additional information
thermal unfolding kinetics and thermal stability, overview
additional information
Bacillus licheniformis is routinely used as a model thermostable amylase, since starch as the substrate is only soluble at tempertures closed to 100°C
additional information
-
Bacillus licheniformis is routinely used as a model thermostable amylase, since starch as the substrate is only soluble at tempertures closed to 100°C
additional information
-
-
additional information
-
Ca2+ and Na+ stabilize at higher reaction temperatures
additional information
-
analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme
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Dobreva, E.; Ivanova, V.
Characterisierung der Strkehydrolysate nach Einwirkung einer thermostabilen alpha-Amylase
Acta Biotechnol.
9
549-554
1989
Bacillus licheniformis, Bacillus licheniformis 44MB82
-
brenda
Bajpai, P.; Bajpai, P.K.
High-temperature alkaline alpha-amylase from Bacillus licheniformis TCRDC-B13
Biotechnol. Bioeng.
33
72-78
1989
Bacillus licheniformis, Bacillus licheniformis TCRDC-B13
brenda
Krishnan, T.; Chandra, A.K.
Purification and characterization of alpha-amylase from Bacillus licheniformis CUMC305
Appl. Environ. Microbiol.
46
430-437
1983
Bacillus licheniformis, Bacillus licheniformis CUMC305
brenda
Kindle, K.L.
Characterization and production of thermostable alpha-amylase
Appl. Biochem. Biotechnol.
8
153-170
1983
Acinetobacter sp., Alicyclobacillus acidocaldarius, Aspergillus niger, Geobacillus stearothermophilus, Bacillus amyloliquefaciens, Weizmannia coagulans, Priestia megaterium, Bacillus subtilis, Bacillus licheniformis, Bacillus sp. (in: Bacteria), Thermochaetoides thermophila, Humicola brevis, Trichocladium griseum, Humicola insolens, Thermomyces lanuginosus, Humicola stellata, Malbranchea pulchella, Micromonospora vulgaris, Rhizomucor miehei, Rhizomucor pusillus, Thermothelomyces myriococcoides, Rhizopus microsporus, Mycothermus thermophilus, Thermomyces dupontii, Thermoactinomyces vulgaris, Thermoascus aurantiacus, Thermoascus crustaceus, Thermomonospora curvata, Thermomonospora viridis, Thermomonospora vulgaris, Bacillus licheniformis CUMC305, Weizmannia coagulans CUMC512, Bacillus sp. (in: Bacteria) 11-15
-
brenda
Morgan, F.J.; Priest, F.G.
Characterization of a thermostable alpha-amylase from Bacillus licheniformis NCIB 6343
J. Appl. Bacteriol.
50
107-114
1981
Bacillus licheniformis, Bacillus licheniformis NCIB 8549, Bacillus licheniformis NCIB 8061, Bacillus licheniformis NCIB 6346, Bacillus licheniformis NCTC 8233, Bacillus licheniformis NCIB 8874, Bacillus licheniformis NCIB 6816, Bacillus licheniformis NCIB 8537, Bacillus licheniformis NCIB 9668, Bacillus licheniformis NCIB 7224
-
brenda
Medda, S.; Chandra, A.K.
New strains of Bacillus licheniformis and Bacillus coagulans producing thermostable alpha-amylase active at alkaline pH
J. Appl. Bacteriol.
48
47-58
1980
Weizmannia coagulans, Bacillus licheniformis, Bacillus licheniformis CUMC305, Weizmannia coagulans CUMC512
brenda
Ingle, M.B.; Erikson, R.J.
Bacterial alpha-amylases
Adv. Appl. Microbiol.
24
257-278
1978
Alicyclobacillus acidocaldarius, Geobacillus stearothermophilus, Weizmannia coagulans, Bacillus licheniformis, Bacillus sp. (in: Bacteria), Clostridium acetobutylicum, Thermomonospora curvata, Alicyclobacillus acidocaldarius 104-1A, Bacillus sp. (in: Bacteria) A-40-2, Alicyclobacillus acidocaldarius Agnano 101
brenda
Svensson, B.
Protein engineering in the alpha-amylase family: catalytic mechanism, substrate specificity and stability
Plant Mol. Biol.
25
141-157
1994
Aspergillus oryzae, Geobacillus stearothermophilus, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus licheniformis, Drosophila melanogaster, Escherichia coli, Saccharomycopsis fibuligera, Homo sapiens, Hordeum vulgare, Mus musculus, Oryza sp., Vigna radiata, Streptomyces hygroscopicus, Sus scrofa, Triticum aestivum, Xanthomonas campestris
brenda
Conrad, B.; Hoang, V.; Polley, A.; Hofemeister, J.
Hybrid Bacillus amyloliquefaciens X Bacillus licheniformis alpha-amylases. Construction, properties and sequence determinants
Eur. J. Biochem.
230
481-490
1995
Bacillus amyloliquefaciens, Bacillus licheniformis
brenda
Dercova, K.; Augustin, J.; Krajcova, D.
Cell growth and alpha-amylase production characteristics of Bacillus subtilis
Folia Microbiol. (Praha)
37
17-23
1991
Geobacillus stearothermophilus, Bacillus subtilis, Bacillus licheniformis, Bacillus licheniformis CCM 2145, Geobacillus stearothermophilus CCM 2183, Bacillus subtilis DP 1
brenda
Shaw, A.; Bott, R.; Day, A.G.
Protein engineering of alpha-amylase for low pH performance
Curr. Opin. Biotechnol.
10
349-352
1999
Bacillus licheniformis (P06278), Bacillus licheniformis
brenda
Khajeh, K.; Nemat-Gorgani, M.
Comparative studies on a mesophilic and a thermophilic alpha-amylase
Appl. Biochem. Biotechnol.
90
47-55
2001
Bacillus amyloliquefaciens, Bacillus licheniformis
brenda
Fitter, J.; Herrmann, R.; Dencher, N.A.; Blume, A.; Hauss, T.
Activity and stability of a thermostable alpha-amylase compared to its mesophilic homologue: mechanisms of thermal adaptation
Biochemistry
40
10723-10731
2001
Bacillus amyloliquefaciens, Bacillus licheniformis (P06278)
brenda
Kainuma, K.
Applied glycoscience-past, present and future
Foods Food Ingredients J. Jpn.
178
4-10
1998
Bacillus licheniformis
-
brenda
Fitter, J.; Haber-Pohlmeier, S.
Structural stability and unfolding properties of thermostable bacterial alpha-amylases: a comparative study of homologous enzymes
Biochemistry
43
9589-9599
2004
Bacillus amyloliquefaciens, Bacillus licheniformis (P06278)
brenda
Bravo Rodriguez, V.; Jurado Alameda, E.; Martinez Gallegos, J.F.; Reyes Requena, A.; Garcia Lopez, A.I.
Enzymatic hydrolysis of soluble starch with an alpha-amylase from Bacillus licheniformis
Biotechnol. Prog.
22
718-722
2006
Bacillus licheniformis
brenda
Mitsuiki, S.; Mukae, K.; Sakai, M.; Goto, M.; Hayashida, S.; Furukawa, K.
Comparative characterization of raw starch hydrolyzing a-amylases from various Bacillus strains
Enzyme Microb. Technol.
37
410-416
2005
Bacillus cereus, Bacillus subtilis, Bacillus licheniformis
-
brenda
Yoon, S.; Robyt, J.F.
Activation and stabilization of 10 starch-degrading enzymes by Triton X-100, polyethylene glycols, and polyvinyl alcohols
Enzyme Microb. Technol.
37
556-562
2005
Aspergillus oryzae, Bacillus amyloliquefaciens, Bacillus licheniformis, Homo sapiens, Sus scrofa
-
brenda
Duy, C.; Fitter, J.
Thermostability of irreversible unfolding alpha-amylases analyzed by unfolding kinetics
J. Biol. Chem.
280
37360-37365
2005
Aspergillus oryzae, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus licheniformis, Sus scrofa
brenda
Ul-Haq, I.; Ashraf, H.; Ali, S.; Qadeer, M.A.
Kinetic characterization of extracellular alpha-amylase from a derepressed mutant of Bacillus licheniformis
Appl. Biochem. Biotechnol.
141
251-264
2007
Bacillus licheniformis, Bacillus licheniformis NA-14
brenda
Bijttebier, A.; Goesaert, H.; Delcour, J.A.
Temperature impacts the multiple attack action of amylases
Biomacromolecules
8
765-772
2007
Aspergillus oryzae, Geobacillus stearothermophilus, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus licheniformis, Sus scrofa, Thermoactinomyces vulgaris
brenda
Ghasemi, A.; Khajeh, K.; Ranjbar, B.
Stabilization of Bacillus licheniformis alpha-amylase by specific antibody which recognizes the N-terminal fragment of the enzyme
Int. J. Biol. Macromol.
41
162-167
2007
Bacillus licheniformis
brenda
Lee, S.; Oneda, H.; Minoda, M.; Tanaka, A.; Inouye, K.
Comparison of starch hydrolysis activity and thermal stability of two Bacillus licheniformis alpha-amylases and insights into engineering alpha-amylase variants active under acidic conditions
J. Biochem.
139
997-1005
2006
Bacillus licheniformis, Bacillus licheniformis IFO12196
brenda
Liu, Y.H.; Lu, F.P.; Li, Y.; Wang, J.L.; Gao, C.
Acid stabilization of Bacillus licheniformis alpha amylase through introduction of mutations
Appl. Microbiol. Biotechnol.
80
795-803
2008
Bacillus licheniformis (P06278), Bacillus licheniformis, Bacillus licheniformis CICC 10181 (P06278)
brenda
Tee, B.L.; Kaletunc, G.
Immobilization of a thermostable alpha-amylase by covalent binding to an alginate matrix increases high temperature usability
Biotechnol. Prog.
25
436-445
2009
Bacillus licheniformis
brenda
Ghalanbor, Z.; Ghaemi, N.; Marashi, S.A.; Amanlou, M.; Habibi-Rezaei, M.; Khajeh, K.; Ranjbar, B.
Binding of Tris to Bacillus licheniformis alpha-amylase can affect its starch hydrolysis activity
Protein Pept. Lett.
15
212-214
2008
Bacillus licheniformis (P06278), Bacillus licheniformis
brenda
Prakash, O.; Jaiswal, N.
alpha-Amylase: an ideal representative of thermostable enzymes
Appl. Biochem. Biotechnol.
160
2401-2414
2010
Alicyclobacillus acidocaldarius, Geobacillus stearothermophilus, Bacillus amyloliquefaciens, Anoxybacillus flavithermus, Bacillus subtilis, Lederbergia lentus, Bacillus licheniformis, Chloroflexus aurantiacus, Thermothelomyces heterothallicus, Desulfurococcus mucosus, Dictyoglomus thermophilum, Thermomyces lanuginosus, Lactiplantibacillus plantarum, Lipomyces kononenkoae, Pyrococcus furiosus, Pyrococcus woesei, Pyrodictium abyssi, Rhizopus sp., Rhodothermus marinus, Mycothermus thermophilus, Staphylothermus marinus, Thermoactinomyces vulgaris, Thermococcus fumicolans, Thermococcus hydrothermalis, Thermococcus litoralis, Thermococcus profundus, Thermotoga maritima, Thermus filiformis, Lactobacillus amylovorus, Halothermothrix orenii, Thermococcus aggregans, Thermococcus celer, Thermococcus guaymasensis
brenda
Rashid, N.; Ahmed, N.; Saleem Haider, M.; Haque, I.
Effective solubilization and single-step purification of Bacillus licheniformis alpha-amylase from insoluble aggregates
Folia Microbiol. (Praha)
55
133-136
2010
Bacillus licheniformis (P06278), Bacillus licheniformis, Bacillus licheniformis ATCC 27811 (P06278)
brenda
Priyadharshini, R.; Manoharan, S.; Hemalatha, D.; Gunasekaran, P.
Repeated random mutagenesis of alpha-amylase from Bacillus licheniformis for improved pH performance
J. Microbiol. Biotechnol.
20
1696-1701
2010
Bacillus licheniformis, Bacillus licheniformis MTCC 6598
brenda
Gashtasbi, F.; Ahmadian, G.; Noghabi, K.A.
New insights into the effectiveness of alpha-amylase enzyme presentation on the Bacillus subtilis spore surface by adsorption and covalent immobilization
Enzyme Microb. Technol.
64-65
17-23
2014
Bacillus licheniformis
brenda
Awasthi, M.K.; Wong, J.W.C.; Kumar, S.; Awasthi, S.K.; Wang, Q.; Wang, M.; Ren, X.; Zhao, J.; Chen, H.; Zhang, Z.
Biodegradation of food waste using microbial cultures producing thermostable alpha-amylase and cellulase under different pH and temperature
Biores. Technol.
248
160-170
2018
Bacillus cereus, Brevibacillus sp., Brevibacillus borstelensis, Bacillus licheniformis (P06278)
brenda
Wu, X.; Wang, Y.; Tong, B.; Chen, X.; Chen, J.
Purification and biochemical characterization of a thermostable and acid-stable alpha-amylase from Bacillus licheniformis B4-423
Int. J. Biol. Macromol.
109
329-337
2018
Bacillus licheniformis, Bacillus licheniformis B4-423
brenda
Homaei, A.; Ghanbarzadeh, M.; Monsef, F.
Biochemical features and kinetic properties of alpha-amylases from marine organisms
Int. J. Biol. Macromol.
83
306-314
2016
Aureobasidium pullulans, Bacillus cereus, Anoxybacillus flavithermus, Bacillus subtilis, Thermomonospora curvata, Thermus sp., Vibrio sp., Eisenia fetida, Saccharopolyspora sp. A9, Wangia sp. C52, Pseudomonas sp. K6-28-040, Anoxybacillus beppuensis, Nocardiopsis sp. B2, Zunongwangia profunda, Rossellomorea aquimaris, Bacillus sp. ALSHL3, Streptomyces sp. D1, Bacillus sp. GM8901, Bacillus sp. TS-23, Bacillus sp. I-3, Bacillus sp. TSCVKK, Bacillus sp. WN 11, Bacillus sp. A-3-15, Chromohalobacter sp. TVSP 101, Bacillus sp. marini, Marinobacter sp. EMB8, Halobacillus sp. amylus, Chryseobacterium taeanense (A0A1G8DI07), Sutcliffiella cohnii (A0A223KY92), Nesterenkonia sp. (A0A2U8ZSD8), Bacillus licheniformis (A1YR25), Bacillus sp. YX-1 (A9YDD9), Parageobacillus caldoxylosilyticus (C0LZ63), Bacillus sp. Ferdowsicous (P86331), Bacillus sp. KSM-K38 (Q93I48), Streptomyces coelicolor A3 (Q9L035), Aureobasidium pullulans N13d, Bacillus subtilis AX20, Chryseobacterium taeanense TKU001 (A0A1G8DI07), Bacillus subtilis DM-03, Anoxybacillus beppuensis TSSC-1, Sutcliffiella cohnii US147 (A0A223KY92), Rossellomorea aquimaris VITP4, Halobacillus sp. amylus HM454199, Parageobacillus caldoxylosilyticus TK4 (C0LZ63), Nesterenkonia sp. F (A0A2U8ZSD8), Streptomyces coelicolor A3 A3(2) (Q9L035), Bacillus licheniformis NH1 (A1YR25), Streptomyces coelicolor A3 M145 (Q9L035), Streptomyces coelicolor A3 ATCC BAA-471 (Q9L035)
brenda
Roy, J.K.; Manhar, A.K.; Nath, D.; Mandal, M.; Mukherjee, A.K.
Cloning and extracellular expression of a raw starch digesting alpha-amylase (Blamy-I) and its application in bioethanol production from a non-conventional source of starch
J. Basic Microbiol.
55
1287-1298
2015
Bacillus licheniformis (I3P686), Bacillus licheniformis, Bacillus licheniformis AS08E (I3P686)
brenda