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Biosynthesis and properties of an extracellular thermostable serine alkaline protease from Virgibacillus pantothenticus.

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Title: Biosynthesis and properties of an extracellular thermostable serine alkaline protease from Virgibacillus pantothenticus.
Authors: Amit Gupta1, Babu Joseph2, Abin Mani2, George Thomas2
Source: World Journal of Microbiology & Biotechnology. Feb2008, Vol. 24 Issue 2, p237-243. 7p.
Subjects: Biochemical templates, Organic synthesis, Biochemistry, Hydrogen-ion concentration
Abstract: Abstract  In this communication, we report the presence of a newly identified serine alkaline protease producing bacteria, Virgibacillus pantothenticus (MTCC 6729) in the fresh chicken meat samples and the factors affecting biosynthesis as well as characterization of protease. The strain produced only 14.3 U ml−1 protease in the standard medium after 72 h of incubation, while in optimized culture conditions the production of protease was increased up to 18.2 U ml−1. The strain was able to produce protease at 40°C at pH 9.0. The addition of dextrose and casein improved protease production. The protease was partially purified and characterized in terms of pH and temperature stability, effect of metal ions and inhibitors. The protease was found to be thermostable alkaline by retaining its 100% and 85% stability at pH 10.0 and at 50°C respectively. The protease was compatible with some of the commercial detergents tested, and was effective in removing protein stains from cotton fabrics. The V. pantothenticus, MTCC 6729 protease appears to be potentially useful as an additive in detergents as a stain remover and other bio-formulations. [ABSTRACT FROM AUTHOR]
Copyright of World Journal of Microbiology & Biotechnology is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Biosynthesis and properties of an extracellular thermostable serine alkaline protease from Virgibacillus pantothenticus.
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  Data: <searchLink fieldCode="AR" term="%22Amit+Gupta%22">Amit Gupta</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Babu+Joseph%22">Babu Joseph</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Abin+Mani%22">Abin Mani</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22George+Thomas%22">George Thomas</searchLink><relatesTo>2</relatesTo>
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  Data: Abstract  In this communication, we report the presence of a newly identified serine alkaline protease producing bacteria, Virgibacillus pantothenticus (MTCC 6729) in the fresh chicken meat samples and the factors affecting biosynthesis as well as characterization of protease. The strain produced only 14.3 U ml−1 protease in the standard medium after 72 h of incubation, while in optimized culture conditions the production of protease was increased up to 18.2 U ml−1. The strain was able to produce protease at 40°C at pH 9.0. The addition of dextrose and casein improved protease production. The protease was partially purified and characterized in terms of pH and temperature stability, effect of metal ions and inhibitors. The protease was found to be thermostable alkaline by retaining its 100% and 85% stability at pH 10.0 and at 50°C respectively. The protease was compatible with some of the commercial detergents tested, and was effective in removing protein stains from cotton fabrics. The V. pantothenticus, MTCC 6729 protease appears to be potentially useful as an additive in detergents as a stain remover and other bio-formulations. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of World Journal of Microbiology & Biotechnology is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Type: general
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              Text: Feb2008
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