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- W2056575983 abstract "Bacillus sp. JER02 is a bacterial strain that can be grown in a medium containing organic solvents and produce a protease enzyme. JER02 protease was purified with a yield of 31.9% of total protein and 328.83-fold purification. K m and Vmax of this protease were established as 0.826 µM and 7.18 µmol/min, respectively. JER02 protease stability was stimulated about 80% by cyclohexane. It exhibited optimum temperature activity at 70°C. Furthermore, this enzyme was active in a wide range of pH (4-12) and showed maximum activity at pH 9.0. The nonionic detergents Tween-20 and Triton X-100 improved the protease activity by 30 and 20%, respectively. In addition, this enzyme was shown to be very stable in the presence of strong anionic surfactants and oxidizing agents, since it retained 77%, 93%, and 98% of its initial activity, after 1 hr of incubation at room temperature with sodium dodecyl sulfate (SDS), sodium perborate (1%, v/v) and H2O2 (1%, v/v), respectively. Overall, the unique properties of the Bacillus sp. JER02 protease suggested that this thermo- and detergent-stable, solvent-tolerant protease has great potential for industrial applications." @default.
- W2056575983 created "2016-06-24" @default.
- W2056575983 creator A5005865017 @default.
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- W2056575983 date "2014-08-19" @default.
- W2056575983 modified "2023-10-18" @default.
- W2056575983 title "Purification and Characterization of a Thermo- and Organic Solvent-Tolerant Alkaline Protease from<i>Bacillus</i>sp. JER02" @default.
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- W2056575983 doi "https://doi.org/10.1080/10826068.2014.907176" @default.
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