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<i>Arthrobacter arilaitensis</i>Re117 as a Source of Solvent-Stable Proteases: Production, Characteristics, Potential Application in the Deproteinization of Shrimp Wastes and Evaluation in Liquid Laundry Commercial Detergents

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Advances in Bioscience and Biotechnology 2015年第2期6卷 105-119页

作者： Rayda Siala Ines Hammemi Sabrine Sellimi Tatiana Vallaeys alya sellami kamoun Moncef Nasri Laboratory of Enzyme Engineering and Microbiology National School of Engineering of Sfax (ENIS) University of Sfax Sfax Tunisia Unité de Recherche Protection des Plantes Cultivées et Environnement Institut de l’Olivier Sfax Tunisia Laboratoire Ecosystèmes Lagunaires UMR 5119 Université de Montpellier Montpellier France

The present study describes the characterization of crude protease extract from Arthrobacter arilaitensis Re117 and its evaluation in solid and liquid detergent. One caseinolytic protease clear band was observed in zymogram. The crude alkaline protease showed optimum activity at pH 9.0 and 50°C, and it was highly stable over a wide range of pH from 8.0 to 9.0. Proteolytic enzymes showed extreme stability towards non-ionic surfactants (Tween 80, Tween 20 and Triton X-100) and stimulate activity towards oxidizing agents such as sodium perborate. They also showed high stability and compatibility with various laundry solid detergents from Tunisian market. The protease of A. arilaitensis Re117, was also tested for shrimp waste deproteinization to produce chitin. The protein removal with a ratio E/S of 20 was about 83%. The novelties of the Re117 protease include its high stability to organic solvents and surfactants. These unique properties make it an ideal choice for application in detergent formulations and enzymatic peptide synthesis. In addition, the enzyme may find potential applications in the deproteinization of shrimp wastes to produce chitin.

关键词： A. arilaitensis Shrimp Wastes Enzymatic Deproteinization Organic Solvent-Stable Protease Laundry Detergents Compatibility

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Optimization of Protease Production by Bacillus mojavensis A21 on Chickpea and Faba Bean

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Advances in Bioscience and Biotechnology 2014年第14期5卷 1049-1060页

作者： Samiha Mhamdi Anissa Haddar Ibtissem Hamza Mnif Fakher Frikha Moncef Nasri alya sellami kamoun Laboratoire de Génie Enzymatique et de Microbiologie Université de Sfax Ecole Nationale d’Ingénieurs de Sfax Sfax Tunisia Université de Sfax Faculté des Sciences de Sfax Sfax Tunisia

Response surface methodology (RSM) was employed to optimize the medium composition and culture conditions for the production of alkaline proteases by Bacillus mojavensis A21 on uncommon substrates: chickpea (CF) and faba bean (FF) flours. A significant positive influence of temperature, CF, FF, incubation time and inoculums size on the protease production was evaluated by Plackett Burman Design. Among these, CF was the most influential factor. The enhancement of protease to 9127 U/ml was achieved with the optimization procedure on the medium composed of (g/l): CF, 40;FF 30, NaCl 2.0;KH2PO4 1;K2HPO4 1;CaCl2, 0.1;MgSO4 0.1. The cultures were conducted for 72 hours with an IS of 2%, at 30°C, an agitation speed of 150 rpm and an initial pH of 8.0. More interestingly, the optimization was accomplished using two cheap and local fermentation substrates, CF and FF, which could result in a significant reduction in the cost of medium constituents. The maximum alkaline protease production was 9127 U/ml after 72 h of incubation and showed 5-fold increase in protease production over the initial level.

关键词： Bacillus mojavensis Protease Chickpea Faba Bean Plackett Burman Design

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