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- W2182826345 abstract "In the present article, we report on the kinetic characterization of enhanced β-amylase production from a derepressed mutant strain of Bacillus subtilis under solid-state fermentation (SSF). For this, six bacterial strains were isolated and screened for enzyme production. Of these, IS-4 exhibited relatively better enzyme production (224.2 U) and hence selected for further improvement through the treatment with ethyl methane sulphonate (EMS) and nitrous acid (NA). Among the mutants, NA-12 gave the highest enzyme activity (451.6 U) and selected for kinetic as well as thermal characterization. M2 (pH 7), as moisture content supported 55% higher amylase activity by the potent mutant in 72 h of incubation. The product yield coefficient (Yp/x = 6.4 U/g) and the specific rate constant (qp = 0.889 U/g/h) using starch as a sole carbon source were many fold improved over to the other carbon sources or strains being used. The purified enzyme was most active at 40C. This enhanced activity remained fairly constant up to a maximum of 44C. NA-induced mutagenesis markedly improved enthalpy (ΔHD = 64.5±4.5 a kJ/mol) and entropy of activation (ΔS = −234±18 ghk J/mol/K) for β-amylase. The substrate binding ability of enzyme for starch hydrolysis was also potentially increased. SDS-PAGE analysis of purified enzyme revealed a single visible protein band corresponding to about 113 kDa mass showing amylase activity. The results have shown an improvement in the endogenous metabolism of mutant strain for β-amylase hyper production (65.55.5 U)." @default.
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- W2182826345 date "2014-01-01" @default.
- W2182826345 modified "2023-09-24" @default.
- W2182826345 title "Kinetic evidence of a thermostable β-amylase from chemically improved mutant strain of Bacillus subtilis." @default.
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