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Enzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT-6 by Arikan Burhan; Unaldi Nisa; Coral Gökhan; Colak Ömer; Aygan Ashabil; Gülnaz Osman is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Enzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT-6 about?
A thermostable alkaline a-amylase producing Bacillus sp. ANT-6 was isolated from soil samples. Enzyme synthesis occurred at temperatures between 25 and 45 8C with an optimum of 37 8C. There was a slight variation in amylase synthesis within the pH range 7 and 11 with an optimum pH of 9. The optimum temperatures for amylase production and growth were the same. Analyses of the enzyme by sodium dodecyl sulphate-polyacrylamide gel electrophoresis revealed a single band, which show amylolytic activity, detected in starch gel. The relative molecular mass of the partial purified enzyme was estimated to be 94 500 Da. The enzyme showed optimum activity at pH 10.5 and 80 8C. The partial purified enzyme was highly active in the alkaline range of pH (9.5 Á/13), and it was completely active up to 100 8C retaining 85.5% initial activity at pH 10.5. Enzyme activity was enhanced in the presence of 5 mM CaCl 2 (110%) and 3 mM PMSF (103%) , and inhibition with 5 mM by Zn, Na, Na-sulphide, EDTA (10 mM), Urea (8 M) and SDS (0.1%) was obtained 36.9, 21.5, 22.2, 4.90, 86% and 10.27, respectively. The enzyme was stable (55%) at high alkaline pH for 24 h. So our result showed that the enzyme was both alka
Who reads Enzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT-6?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Arikan Burhan; Unaldi Nisa; Coral Gökhan; Colak Ömer; Aygan Ashabil; Gülnaz Osman
- Publisher
- Elsevier Science; Elsevier ; Elsevier Applied Science; Elsevier BV (ISSN 1873-3298)
- Published
- 2003
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)