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- W1524150295 abstract "A halotolerant α-amylase having the ability of digesting the insoluble raw starches was characterized from Bacillus subtilis S8-18, a marine sediment isolate from Palk Bay region. The electrophoresis techniques unveiled that the α-amylase was indeed a monomer with a molecular weight of 57 kDa. The optimum temperature and pH for the enzyme activity were 60 °C and 6.0 respectively. The enzyme was highly stable for 24 h over a wide range of pH from 4.0 to 12.0 by showing 84-94% activity. Interestingly, by retaining 72% activity even after 24 h, the enzyme also showed tolerance towards 28% NaCl. The α-amylase retained a minimum of 93% residual activity in 1 mM concentration for the selected divalent metal ions. The enzyme was found to be chelator resistant as it remained unaffected by 1 mM of EDTA and exhibited 96% activity even at 5 mM concentration. Furthermore, though 1% SDS caused remarkable reduction (68%) in amylase activity, the enzyme showed tolerance towards other detergents (1% of Triton-X and Tween 80) with 85% activity. Additionally, the α-amylase enzyme is capable of hydrolyzing the insoluble raw starch substrates which was evident from the scanning electron microscopic (SEM) and spectrophotometric analyses." @default.
- W1524150295 created "2016-06-24" @default.
- W1524150295 creator A5033318120 @default.
- W1524150295 creator A5060964743 @default.
- W1524150295 date "2013-05-26" @default.
- W1524150295 modified "2023-10-14" @default.
- W1524150295 title "Halotolerant, acid‐alkali stable, chelator resistant and raw starch digesting α‐amylase from a marine bacterium <i>Bacillus subtilis</i> S8–18" @default.
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- W1524150295 doi "https://doi.org/10.1002/jobm.201200732" @default.
- W1524150295 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23712833" @default.
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