Genomic and exoproteomic analyses of cold‐ and alkaline‐adapted bacteria reveal an abundance of secreted subtilisin‐like proteases
Proteases active at low temperature or high pH are used in many commercial applications, including the detergent, food and feed industries, and bacteria specifically adapted to these conditions are a potential source of novel proteases. Environments combining these two extremes are very rare, but of...
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ftpubmed:oai:pubmedcentral.nih.gov:4767292 2023-05-15T14:03:58+02:00 Genomic and exoproteomic analyses of cold‐ and alkaline‐adapted bacteria reveal an abundance of secreted subtilisin‐like proteases Lylloff, Jeanette E. Hansen, Lea B.S. Jepsen, Morten Sanggaard, Kristian W. Vester, Jan K. Enghild, Jan J. Sørensen, Søren J. Stougaard, Peter Glaring, Mikkel A. 2016-02-01 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4767292/ http://www.ncbi.nlm.nih.gov/pubmed/26834075 https://doi.org/10.1111/1751-7915.12343 en eng John Wiley and Sons Inc. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4767292/ http://www.ncbi.nlm.nih.gov/pubmed/26834075 http://dx.doi.org/10.1111/1751-7915.12343 © 2016 The Authors. Microbial Biotechnology published by John Wiley & Sons Ltd and Society for Applied Microbiology. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. CC-BY Research Articles Text 2016 ftpubmed https://doi.org/10.1111/1751-7915.12343 2016-03-27T01:02:11Z Proteases active at low temperature or high pH are used in many commercial applications, including the detergent, food and feed industries, and bacteria specifically adapted to these conditions are a potential source of novel proteases. Environments combining these two extremes are very rare, but offer the promise of proteases ideally suited to work at both high pH and low temperature. In this report, bacteria from two cold and alkaline environments, the ikaite columns in Greenland and alkaline ponds in the McMurdo Dry Valley region, Antarctica, were screened for extracellular protease activity. Two isolates, Arsukibacterium ikkense from Greenland and a related strain, Arsukibacterium sp. MJ3, from Antarctica, were further characterized with respect to protease production. Genome sequencing identified a range of potential extracellular proteases including a number of putative secreted subtilisins. An extensive liquid chromatography–tandem mass spectrometry analysis of proteins secreted by A. ikkense identified six subtilisin‐like proteases as abundant components of the exoproteome in addition to other peptidases potentially involved in complete degradation of extracellular protein. Screening of Arsukibacterium genome libraries in Escherichia coli identified two orthologous secreted subtilisins active at pH 10 and 20°C, which were also present in the A. ikkense exoproteome. Recombinant production of both proteases confirmed the observed activity. Text Antarc* Antarctica Greenland PubMed Central (PMC) Greenland Microbial Biotechnology 9 2 245 256 |
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Research Articles |
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Research Articles Lylloff, Jeanette E. Hansen, Lea B.S. Jepsen, Morten Sanggaard, Kristian W. Vester, Jan K. Enghild, Jan J. Sørensen, Søren J. Stougaard, Peter Glaring, Mikkel A. Genomic and exoproteomic analyses of cold‐ and alkaline‐adapted bacteria reveal an abundance of secreted subtilisin‐like proteases |
topic_facet |
Research Articles |
description |
Proteases active at low temperature or high pH are used in many commercial applications, including the detergent, food and feed industries, and bacteria specifically adapted to these conditions are a potential source of novel proteases. Environments combining these two extremes are very rare, but offer the promise of proteases ideally suited to work at both high pH and low temperature. In this report, bacteria from two cold and alkaline environments, the ikaite columns in Greenland and alkaline ponds in the McMurdo Dry Valley region, Antarctica, were screened for extracellular protease activity. Two isolates, Arsukibacterium ikkense from Greenland and a related strain, Arsukibacterium sp. MJ3, from Antarctica, were further characterized with respect to protease production. Genome sequencing identified a range of potential extracellular proteases including a number of putative secreted subtilisins. An extensive liquid chromatography–tandem mass spectrometry analysis of proteins secreted by A. ikkense identified six subtilisin‐like proteases as abundant components of the exoproteome in addition to other peptidases potentially involved in complete degradation of extracellular protein. Screening of Arsukibacterium genome libraries in Escherichia coli identified two orthologous secreted subtilisins active at pH 10 and 20°C, which were also present in the A. ikkense exoproteome. Recombinant production of both proteases confirmed the observed activity. |
format |
Text |
author |
Lylloff, Jeanette E. Hansen, Lea B.S. Jepsen, Morten Sanggaard, Kristian W. Vester, Jan K. Enghild, Jan J. Sørensen, Søren J. Stougaard, Peter Glaring, Mikkel A. |
author_facet |
Lylloff, Jeanette E. Hansen, Lea B.S. Jepsen, Morten Sanggaard, Kristian W. Vester, Jan K. Enghild, Jan J. Sørensen, Søren J. Stougaard, Peter Glaring, Mikkel A. |
author_sort |
Lylloff, Jeanette E. |
title |
Genomic and exoproteomic analyses of cold‐ and alkaline‐adapted bacteria reveal an abundance of secreted subtilisin‐like proteases |
title_short |
Genomic and exoproteomic analyses of cold‐ and alkaline‐adapted bacteria reveal an abundance of secreted subtilisin‐like proteases |
title_full |
Genomic and exoproteomic analyses of cold‐ and alkaline‐adapted bacteria reveal an abundance of secreted subtilisin‐like proteases |
title_fullStr |
Genomic and exoproteomic analyses of cold‐ and alkaline‐adapted bacteria reveal an abundance of secreted subtilisin‐like proteases |
title_full_unstemmed |
Genomic and exoproteomic analyses of cold‐ and alkaline‐adapted bacteria reveal an abundance of secreted subtilisin‐like proteases |
title_sort |
genomic and exoproteomic analyses of cold‐ and alkaline‐adapted bacteria reveal an abundance of secreted subtilisin‐like proteases |
publisher |
John Wiley and Sons Inc. |
publishDate |
2016 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4767292/ http://www.ncbi.nlm.nih.gov/pubmed/26834075 https://doi.org/10.1111/1751-7915.12343 |
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Greenland |
geographic_facet |
Greenland |
genre |
Antarc* Antarctica Greenland |
genre_facet |
Antarc* Antarctica Greenland |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4767292/ http://www.ncbi.nlm.nih.gov/pubmed/26834075 http://dx.doi.org/10.1111/1751-7915.12343 |
op_rights |
© 2016 The Authors. Microbial Biotechnology published by John Wiley & Sons Ltd and Society for Applied Microbiology. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.1111/1751-7915.12343 |
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Microbial Biotechnology |
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9 |
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2 |
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245 |
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256 |
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1766274890823892992 |