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Biotechnology of Cold-Active Proteases
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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3960895/ https://www.ncbi.nlm.nih.gov/pubmed/24832807 http://dx.doi.org/10.3390/biology2020755 |
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author | Joshi, Swati Satyanarayana, Tulasi |
author_facet | Joshi, Swati Satyanarayana, Tulasi |
author_sort | Joshi, Swati |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3960895 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-39608952014-05-07 Biotechnology of Cold-Active Proteases Joshi, Swati Satyanarayana, Tulasi Biology (Basel) Review 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. MDPI 2013-05-03 /pmc/articles/PMC3960895/ /pubmed/24832807 http://dx.doi.org/10.3390/biology2020755 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Joshi, Swati Satyanarayana, Tulasi Biotechnology of Cold-Active Proteases |
title | Biotechnology of Cold-Active Proteases |
title_full | Biotechnology of Cold-Active Proteases |
title_fullStr | Biotechnology of Cold-Active Proteases |
title_full_unstemmed | Biotechnology of Cold-Active Proteases |
title_short | Biotechnology of Cold-Active Proteases |
title_sort | biotechnology of cold-active proteases |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3960895/ https://www.ncbi.nlm.nih.gov/pubmed/24832807 http://dx.doi.org/10.3390/biology2020755 |
work_keys_str_mv | AT joshiswati biotechnologyofcoldactiveproteases AT satyanarayanatulasi biotechnologyofcoldactiveproteases |