Genomic and exoproteomic analyses of cold- and alkaline-adapted bacteria reveal an abundance of secreted subtilisin-like proteases
| Autor: | Peter Stougaard, Søren J. Sørensen, Morten Jepsen, Jan Kjølhede Vester, Kristian W. Sanggaard, Lea Benedicte Skov Hansen, Mikkel A. Glaring, Jan J. Enghild, Jeanette E. Lylloff |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Proteomics Proteases medicine.medical_treatment 030106 microbiology Greenland Antarctic Regions Bioengineering Biology Alkalies medicine.disease_cause Applied Microbiology and Biotechnology Biochemistry Genome Chromatiaceae 03 medical and health sciences Tandem Mass Spectrometry Extracellular medicine Environmental Microbiology Escherichia coli Subtilisins Research Articles Protease fungi Subtilisin Computational Biology Genomics Sequence Analysis DNA biology.organism_classification Cold Temperature 030104 developmental biology Bacteria Biotechnology Chromatography Liquid |
| Zdroj: | 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 Microbial Biotechnology |
| DOI: | 10.1111/1751-7915.12343 |
| Popis: | Summary 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. |
| Databáze: | OpenAIRE |
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