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• W2074749251 endingPage "1798" @default.
• W2074749251 startingPage "1791" @default.
• W2074749251 abstract "Anoxybacillus beppuensis TSSC-1 (GenBank Number, EU710556), a thermophilic bacterium isolated from a hot spring reservoir, was found to optimally secrete a monomeric α-amylase at 55 °C and pH 7. The enzyme was purified to homogeneity by a single-step purification on phenyl sepharose 6FF, achieving a 58% yield, 10,000 U/mg specific activity and 19.5 fold purification. The molecular weight, Km and Vmax were 43 kD, 0.5 mg ml−1 and 3571.42 μmol ml−1 m−1, respectively. The enzymatic catalysis of soluble starch was optimum at 80 °C and pH 7. The thermodynamic parameters, Kd, t1/2, ΔH*, ΔS*, E and ΔG*, were consistent. The very compact structure of the enzyme and the transitional enzyme–substrate complex resisted denaturation at extreme temperatures and alkaline pH. The Kd and t1/2 measurements were consistent with the high thermostability and pH tolerance observed. The structural stability of the enzyme was also reflected by the values of ΔH*, ΔS*, E and ΔG*. While the enzyme did not exhibit metal ion dependency, it was resistant to chemical denaturation. The broad thermo- and pH-tolerance of this enzyme suggests potential commercial opportunities." @default.
• W2074749251 created "2016-06-24" @default.
• W2074749251 creator A5005684994 @default.
• W2074749251 creator A5022928888 @default.
• W2074749251 date "2012-12-01" @default.
• W2074749251 modified "2023-09-25" @default.
• W2074749251 title "The stability and thermodynamic parameters of a very thermostable and calcium-independent α-amylase from a newly isolated bacterium, Anoxybacillus beppuensis TSSC-1" @default.
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• W2074749251 doi "https://doi.org/10.1016/j.procbio.2012.06.005" @default.
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