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Engineering of the α-amylase from Geobacillus stearothermophilus US100 for detergent incorporation

Authors

  • Bassem Khemakhem,

    1. Centre de Biotechnologie de Sfax B.P. “K” 3038 Sfax, Tunisie; telephone: 216-74-440-451; fax: 216-74-440-451
    2. Laboratoire de BioCristallographie, Institut de Biologie et Chimie des Protéines, UMR 5086-CNRS/Université de Lyon, IFR128 “BioSciences Lyon-Gerland”, 7 Passage du Vercors, F-69367 Lyon Cedex 07, France
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  • Mamdouh Ben Ali,

    Corresponding author
    1. Centre de Biotechnologie de Sfax B.P. “K” 3038 Sfax, Tunisie; telephone: 216-74-440-451; fax: 216-74-440-451
    • Centre de Biotechnologie de Sfax B.P. “K” 3038 Sfax, Tunisie; telephone: 216-74-440-451; fax: 216-74-440-451.
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  • Nushin Aghajari,

    1. Laboratoire de BioCristallographie, Institut de Biologie et Chimie des Protéines, UMR 5086-CNRS/Université de Lyon, IFR128 “BioSciences Lyon-Gerland”, 7 Passage du Vercors, F-69367 Lyon Cedex 07, France
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  • Michel Juy,

    1. Laboratoire de BioCristallographie, Institut de Biologie et Chimie des Protéines, UMR 5086-CNRS/Université de Lyon, IFR128 “BioSciences Lyon-Gerland”, 7 Passage du Vercors, F-69367 Lyon Cedex 07, France
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  • Richard Haser,

    1. Laboratoire de BioCristallographie, Institut de Biologie et Chimie des Protéines, UMR 5086-CNRS/Université de Lyon, IFR128 “BioSciences Lyon-Gerland”, 7 Passage du Vercors, F-69367 Lyon Cedex 07, France
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  • Samir Bejar

    1. Centre de Biotechnologie de Sfax B.P. “K” 3038 Sfax, Tunisie; telephone: 216-74-440-451; fax: 216-74-440-451
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Abstract

AmyUS100ΔIG is a variant of the most thermoactive and thermostable maltohexaose forming α-amylase produced by Geobacillus stearothermophilus sp.US100. This enzyme which was designed to improve the thermostability of the wild-type enzyme has acquired a very high resistance to chelator agents. According to modeling structural studies and with the aim of enhancing its resistance towards chemical oxidation, a mutant (AmyUS100ΔIG/M197A) was created by substituting methionine 197 to alanine. The catalytic proprieties of the resulting mutant show alterations in the specific activity and the profile of starch hydrolysis. Interestingly, AmyUS100ΔIG/M197A displayed the highest resistance to oxidation compared to the AmyUS100ΔIG and to Termamyl300®, the well-known commercial amylase used in detergent. Further, performance of the engineered α-amylase was estimated in the presence of commonly used detergent compounds and a wide range of commercial detergent (liquid and solid). These studies indicated a high compatibility and performance of AmyUS100ΔIG/M197A, suggesting its potential application in detergent industry. Biotechnol. Bioeng. 2009;102: 380–389. © 2008 Wiley Periodicals, Inc.

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