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Molecular characterization of a proteolysis-resistant lipase from Bacillus pumilus SG2
Proteolysis-resistant lipases can be well exploited by industrial processes which employ both lipase and protease as biocatalysts. A proteolysis resistant lipase from Bacillus pumilus SG2 was isolated, purified and characterized earlier. The lipase was resistant to native and commercial proteases. I...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Sociedade Brasileira de Microbiologia
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4166261/ https://www.ncbi.nlm.nih.gov/pubmed/25242920 |
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author | Sangeetha, R. Arulpandi, I. Geetha, A. |
author_facet | Sangeetha, R. Arulpandi, I. Geetha, A. |
author_sort | Sangeetha, R. |
collection | PubMed |
description | Proteolysis-resistant lipases can be well exploited by industrial processes which employ both lipase and protease as biocatalysts. A proteolysis resistant lipase from Bacillus pumilus SG2 was isolated, purified and characterized earlier. The lipase was resistant to native and commercial proteases. In the present work, we have characterized the lip gene which encodes the proteolysis-resistant lipase from Bacillus pumilus SG2. The parameters and structural details of lipase were analysed. The lip gene consisted of 650 bp. The experimental molecular weight of SG2 lipase was nearly double that of its theoretical molecular weight, thus suggesting the existence of the functional lipase as a covalent dimer. The proteolytic cleavage sites of the lipase would have been made inaccessible by dimerisation, thus rendering the lipase resistant to protease. |
format | Online Article Text |
id | pubmed-4166261 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Sociedade Brasileira de Microbiologia |
record_format | MEDLINE/PubMed |
spelling | pubmed-41662612014-09-29 Molecular characterization of a proteolysis-resistant lipase from Bacillus pumilus SG2 Sangeetha, R. Arulpandi, I. Geetha, A. Braz J Microbiol Industrial Microbiology Proteolysis-resistant lipases can be well exploited by industrial processes which employ both lipase and protease as biocatalysts. A proteolysis resistant lipase from Bacillus pumilus SG2 was isolated, purified and characterized earlier. The lipase was resistant to native and commercial proteases. In the present work, we have characterized the lip gene which encodes the proteolysis-resistant lipase from Bacillus pumilus SG2. The parameters and structural details of lipase were analysed. The lip gene consisted of 650 bp. The experimental molecular weight of SG2 lipase was nearly double that of its theoretical molecular weight, thus suggesting the existence of the functional lipase as a covalent dimer. The proteolytic cleavage sites of the lipase would have been made inaccessible by dimerisation, thus rendering the lipase resistant to protease. Sociedade Brasileira de Microbiologia 2014-08-29 /pmc/articles/PMC4166261/ /pubmed/25242920 Text en Copyright © 2014, Sociedade Brasileira de Microbiologia All the content of the journal, except where otherwise noted, is licensed under a Creative Commons License CC BY-NC. |
spellingShingle | Industrial Microbiology Sangeetha, R. Arulpandi, I. Geetha, A. Molecular characterization of a proteolysis-resistant lipase from Bacillus pumilus SG2 |
title | Molecular characterization of a proteolysis-resistant lipase from Bacillus pumilus SG2 |
title_full | Molecular characterization of a proteolysis-resistant lipase from Bacillus pumilus SG2 |
title_fullStr | Molecular characterization of a proteolysis-resistant lipase from Bacillus pumilus SG2 |
title_full_unstemmed | Molecular characterization of a proteolysis-resistant lipase from Bacillus pumilus SG2 |
title_short | Molecular characterization of a proteolysis-resistant lipase from Bacillus pumilus SG2 |
title_sort | molecular characterization of a proteolysis-resistant lipase from bacillus pumilus sg2 |
topic | Industrial Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4166261/ https://www.ncbi.nlm.nih.gov/pubmed/25242920 |
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