Reversibility of Heat-Inactivation of Bacillus subtilis' α-Amylase
نویسندگان
چکیده
منابع مشابه
Bottleneck in secretion of α-amylase in Bacillus subtilis
Amylase plays an important role in biotechnology industries, and Gram-positive bacterium Bacillus subtilis is a major host to produce heterogeneous α-amylases. However, the secretion stress limits the high yield of α-amylase in B. subtilis although huge efforts have been made to address this secretion bottleneck. In this question-oriented review, every effort is made to answer the following que...
متن کاملThe Theoretical Study on a Nano Biosystem Consisting of Nano Tube-Catalytic Site of Bacillus Subtilis α-Amylase, PDB: 1UA7
α-Amylase has been studied extensively from various sides. This enzyme is used in many industries .Many applications of this enzyme have encouraged us for greater attempts on the study of α-amylase and to search for more effective processes. In this investigation, the structure of nanotube - catalytic site of bacillus subtilis α- amylase was optimized by hype...
متن کاملHeterologous expression, biochemical characterization, and overproduction of alkaline α-amylase from Bacillus alcalophilus in Bacillus subtilis
BACKGROUND Alkaline α-amylases have potential applications for hydrolyzing starch under high pH conditions in the starch and textile industries and as ingredients in detergents for automatic dishwashers and laundries. While the alkaline α-amylase gains increased industrial interest, the yield of alkaline α-amylases from wild-type microbes is low, and the combination of genetic engineering and p...
متن کاملThe inactivation of Bacillus subtilis alpha-amylase by N-acetylimidazole and tetranitromethane.
Bacillus subtilis oc-amylase is inactivated by treatment with N-acetylimidazole. Full catalytic activity is restored when the acetylated protein is treated with hydroxylamine. Spectral changes associated with the loss and recovery of activity indicate that exposed residues of tyrosine react. I f the enzyme is acetylated in the presence of substrate (soluble starch) the modified protein retains ...
متن کاملThe Chemical Modification of α-Amylase from Locale Bacteria of Bacillus subtilis ITBCCB148 using Citraconic Anhydride
Chemical modification of α-amylase from locale bacteria isolate Bacillus subtilis ITBCCB148 using citraconic anhydride has been performed. increase thermal stability of the enzyme has successfully been done. The results showed that the modified enzymes with citraconic anhydride with modification degree of 45, 73, 82, 83, and 88% have similar optimum pH of 5.5 and optimum temperature of 60°C; ki...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1966
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.30.994