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Overexpression and characterization of an esterase from Streptomyces diastatochromogenes

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Abstract

Highest overexpression of an esterase from Streptomyces diastatochromogenes (EstA) cloned into E. coli was achieved using a rhamnose-inducible promotor. Highest activity (175 U/ml) was observed 5 h after induction. The lyophilized enzyme had a specific activity of 150 U/mg towards p-nitrophenyl acetate and 48 U/mg towards ethyl acetate. EstA was active in a wide range of pH (optimal 7.5) and temperature (optimal 44 °C ) but became unstable above 50 °C. EstA exibited modest enantioselectivity in the hydrolysis of α-phenylethyl acetate.

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Authors and Affiliations

  1. Institut für Technische Biochemie, Universität Stuttgart, Allmandring 31, D-70569, Stuttgart, Germany

    Vlada Khalameyzer & Uwe T. Bornscheuer

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  1. Vlada Khalameyzer
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  2. Uwe T. Bornscheuer
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Khalameyzer, V., Bornscheuer, U.T. Overexpression and characterization of an esterase from Streptomyces diastatochromogenes . Biotechnology Letters 21, 101–104 (1999). https://doi.org/10.1023/A:1005445214284

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  • DOI: https://doi.org/10.1023/A:1005445214284

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