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Asian Journal of Biotechnology
  Year: 2011 | Volume: 3 | Issue: 1 | Page No.: 58-67
DOI: 10.3923/ajbkr.2011.58.67
 
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A Novel Thermostable Alkaline α-Amylase from Bacillus circulans PN5: Biochemical Characterization and Production

B.H. Joshi

Abstract:
Amylase (1-4, α-D glucan glucanohydrolase E C 3.2.1.1) hydrolyses α-1,4 glucosidic linkage in starch and related substrates in an endofashion producing oligosaccharides, glucose and α-limit dextrin. In this study, 56 potential bacterial isolates of amylase producer were obtained during the primary screening. Secondary screening of these isolates yielded a highly thermostable alkaline α-amylase producing isolates identified as Bacillus circulans PN5. This strain was found to produce 36 U mL-1 of thermostable amylase at pH 10. Amylase was further evaluated for its biochemical properties such as pH optima, temperature optima and stability. Results showed that the enzyme was produced in the pH range of 8-11 with pH optima at 10. The enzyme was found to retain more than 60% residual activity in the pH range of pH 7-12. The optimum temperature for enzyme production was 80°C at pH 10. When starch as a carbon and peptone as a nitrogen source were used in production medium, the enzyme yield was increased. These parametric optimization resulted in to the significant increase in the enzyme production with a maximum of 48 U mL-1. The enzyme was highly stable with commercial detergents tested. These studies confirmed the suitability of enzymes for various applications such as starch processing, detergent formulations and many other related industries.
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How to cite this article:

B.H. Joshi , 2011. A Novel Thermostable Alkaline α-Amylase from Bacillus circulans PN5: Biochemical Characterization and Production. Asian Journal of Biotechnology, 3: 58-67.

DOI: 10.3923/ajbkr.2011.58.67

URL: https://scialert.net/abstract/?doi=ajbkr.2011.58.67

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