Exploration of detergent-stable alkaline α-amylase AA7 from Bacillus sp strain SP-CH7 isolated from Chilika Lake.

Int J Biol Macromol

Department of Microbiology, C.B.S.H., Orissa University of Agriculture and Technology, Unit 7, Surya Nagar, Bhubaneshwar, Odisha 751003, India.

Published: November 2019

AI Article Synopsis

  • A bacterial isolate (CH7) from Chilika Lake sediments produces α-amylase at high pH levels, specifically at pH 11.0, showing significant enzyme activity and survival in high salt concentrations.
  • Taxonomically identified as Bacillus sp. strain SP-CH7, the enzyme demonstrated impressive characteristics with a specific activity of 202.857 IU/mg and stability across a range of alkaline conditions, particularly pH 11.0 and 13.0.
  • The enzyme displays potential applications in the detergent industry due to its stability in the presence of various detergents and its enzyme activity being enhanced by certain metal ions like Co, Na, and Ca.

Article Abstract

An alkali-tolerant bacterial isolate CH7 was isolated from Chilika Lake sediments that produced α-amylase at high pH. It showed >15 mm zone diameter at pH 11.0 on agar plate containing 1% starch hence considered for study. It survived up to 10% NaCl concentration on nutrient agar plates. Taxonomically it was identified as Bacillus sp. strain SP-CH7 having GenBank Accession No. KU761266. Optimized alkaline α-amylase, AA7 showed 202.857 specific activity (IU/mg), 65.95 purification fold and 25.94 yield (%) respectively. Molecular weight was revealed by SDS-PAGE as 55 kDa. The K value was 0.688 mg/mL and so was 2.342 IU/mL V obtained for AA7 towards starch. This enzyme showed 92.79% and 91.14% stability at pH 11.0 and 13.0 respectively and up to 75 °C stability was also noted. Enzyme activity was stimulated by Co, Na and Ca. It was stable in presence of EDTA, SDS, all the powdered detergents as well as with liquid detergent "Ezee" which vouches for its potential application in Detergent industries.

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http://dx.doi.org/10.1016/j.ijbiomac.2019.08.006DOI Listing

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