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Psychrophily and Catalysis
Biology 2013, 2(2), 755-783; doi:10.3390/biology2020755

Biotechnology of Cold-Active Proteases

Department of Microbiology, University of Delhi South Campus, New Delhi 110021, India
* Author to whom correspondence should be addressed.
Received: 5 March 2013 / Revised: 17 April 2013 / Accepted: 24 April 2013 / Published: 3 May 2013
(This article belongs to the Special Issue Polar Microbiology: Recent Advances and Future Perspectives)
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The bulk of Earth’s biosphere is cold (<5 °C) and inhabited by psychrophiles. Biocatalysts from psychrophilic organisms (psychrozymes) have attracted attention because of their application in the ongoing efforts to decrease energy consumption. Proteinases as a class represent the largest category of industrial enzymes. There has been an emphasis on employing cold-active proteases in detergents because this allows laundry operations at ambient temperatures. Proteases have been used in environmental bioremediation, food industry and molecular biology. In view of the present limited understanding and availability of cold-active proteases with diverse characteristics, it is essential to explore Earth’s surface more in search of an ideal cold-active protease. The understanding of molecular and mechanistic details of these proteases will open up new avenues to tailor proteases with the desired properties. A detailed account of the developments in the production and applications of cold-active proteases is presented in this review.
Keywords: Extremozymes; psychrozymes; cold-active protease; metagenomics; site directed mutagenesis; x-ray crystallography Extremozymes; psychrozymes; cold-active protease; metagenomics; site directed mutagenesis; x-ray crystallography
This is an open access article distributed under the Creative Commons Attribution License (CC BY) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Joshi, S.; Satyanarayana, T. Biotechnology of Cold-Active Proteases. Biology 2013, 2, 755-783.

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