Protein engineering of bacterial α-amylases

Nielsen, Jens Erik; Borchert, Torben V.

doi:10.1016/s0167-4838(00)00240-5

Cited by 252 publications

(166 citation statements)

References 78 publications

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“…The properties of each α-amylase such as thermostability, pH profile, pH stability, and Ca-independency must be matched to its application. For example, α-amylases used in starch industry must be active and stable at low pH but in detergent industry at high pH values (19).…”

Section: Introductionmentioning

confidence: 99%

Properties of an amylase from thermophilic Bacillus SP.

Carvalho

Corrêa

Silva

et al. 2008

Braz. J. Microbiol.

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α-Amylase production by thermophilic Bacillus sp strain SMIA-2 cultivated in liquid cultures containing soluble starch as a carbon source and supplemented with 0.05% whey protein and 0.2% peptone reached a maximum activity at 32 h, with levels of 37 U/mL. Studies on the amylase characterization revealed that the optimum temperature of this enzyme was 90ºC. The enzyme was stable for 1 h at temperatures ranging from 40-50ºC while at 90ºC, 66% of its maximum activity was lost. However, in the presence of 5 mM CaCl2, the enzyme was stable at 90ºC for 30 min and retained about 58% residual activity after 1 h. The optimum pH of the enzyme was found to be 8.5. After incubation of enzyme for 2 h at pH 9.5 and 11.0 was observed a decrease of about 6.3% and 16.5% of its original activity. At pH 6.0 the enzyme lost about 36% of its original activity. . In the presence of 2.0 M NaCl, 63% of amylase activity was retained after 2 h incubation at 45ºC. The amylase exhibited more than 70% activity when incubated for 1 h at 50ºC with sodium dodecyl sulphate. However, very little residual activity was obtained with sodium hypochlorite and with hydrogen peroxide the enzyme was completely inhibited. The compatibility of Bacillus sp SMIA-2 amylase with certain commercial detergents was shown to be good as the enzyme retained 86%, 85% and 75% of its activity after 20 min incubation at 50ºC in the presence of the detergent brands Omo ® , Campeiro ® and Tide ® , respectively.

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Section: Introductionmentioning

confidence: 99%

Properties of an amylase from thermophilic Bacillus SP.

Carvalho

Corrêa

Silva

et al. 2008

Braz. J. Microbiol.

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“…Distribution of -amylase is wide from common mesophilic bacteria to hyperthermophilic archaeon Pyrococcus furiosus (Jorgensen et al, 1997). Alpha-amylase of B. subtilis is used commercially in various categories such as starch hydrolysis in starch liquefaction process and additives to detergents for both washing machines and automated dish-washers because of its high thermo-stable activity (Nielsen & Borchert, 2000). As -amylase, which catalyzes the hydrolysis and transglycosylation at -1,4-and -1,6-glycosidic linkages, it doesn't seem to be responsible for degradation of xylan.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Enzymes Associated with Degradation of Insoluble Fiber of Soybean Curd Residue by Bacillus subtilis

Shoda¹,

Mizumoto²

2011

Recent Trends for Enhancing the Diversity and Quality of Soybean Products

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“…This is because of their capacity to catalyze reactions under environmentally friendly conditions and without the addition of expensive activated sugars (Buchholz & Seibel, 2008). In the sugar-producing industry (Nielsen & Borchert, 2000), bacterial and fungal -amylases of family GH13, particularly those of the Bacillus species, play a vital role in the starch liquefaction process. Starch from wheat, maize and tapioca is hydrolyzed to produce oligosaccharides by the thermostable -amylases from Bacillus licheniformis.…”

Section: Alpha-amylasesmentioning

confidence: 99%