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...
Published in: | Microbial Biotechnology |
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ftuniaarhuspubl:oai:pure.atira.dk:publications/8be475d6-3781-4105-81b2-334a10468717 2023-05-15T13:51:30+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 https://pure.au.dk/portal/da/publications/genomic-and-exoproteomic-analyses-of-cold-and-alkalineadapted-bacteria-reveal-an-abundance-of-secreted-subtilisinlike-proteases(8be475d6-3781-4105-81b2-334a10468717).html https://doi.org/10.1111/1751-7915.12343 eng eng info:eu-repo/semantics/openAccess Lylloff , J E , Hansen , L B S , Jepsen , M , Sanggaard , K W , Vester , J K , Enghild , J J , Sørensen , S J , Stougaard , P & Glaring , M A 2016 , ' Genomic and exoproteomic analyses of cold- and alkaline-adapted bacteria reveal an abundance of secreted subtilisin-like proteases ' , Microbial Biotechnology , vol. 9 , no. 2 , pp. 245-256 . https://doi.org/10.1111/1751-7915.12343 article 2016 ftuniaarhuspubl https://doi.org/10.1111/1751-7915.12343 2020-10-21T22:45:20Z 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. Article in Journal/Newspaper Antarc* Antarctica Greenland Aarhus University: Research Greenland Microbial Biotechnology 9 2 245 256 |
institution |
Open Polar |
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Aarhus University: Research |
op_collection_id |
ftuniaarhuspubl |
language |
English |
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 |
Article in Journal/Newspaper |
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 |
spellingShingle |
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 |
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 |
publishDate |
2016 |
url |
https://pure.au.dk/portal/da/publications/genomic-and-exoproteomic-analyses-of-cold-and-alkalineadapted-bacteria-reveal-an-abundance-of-secreted-subtilisinlike-proteases(8be475d6-3781-4105-81b2-334a10468717).html https://doi.org/10.1111/1751-7915.12343 |
geographic |
Greenland |
geographic_facet |
Greenland |
genre |
Antarc* Antarctica Greenland |
genre_facet |
Antarc* Antarctica Greenland |
op_source |
Lylloff , J E , Hansen , L B S , Jepsen , M , Sanggaard , K W , Vester , J K , Enghild , J J , Sørensen , S J , Stougaard , P & Glaring , M A 2016 , ' Genomic and exoproteomic analyses of cold- and alkaline-adapted bacteria reveal an abundance of secreted subtilisin-like proteases ' , Microbial Biotechnology , vol. 9 , no. 2 , pp. 245-256 . https://doi.org/10.1111/1751-7915.12343 |
op_rights |
info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.1111/1751-7915.12343 |
container_title |
Microbial Biotechnology |
container_volume |
9 |
container_issue |
2 |
container_start_page |
245 |
op_container_end_page |
256 |
_version_ |
1766255381037711360 |