Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B
Here we employed sequence-based and structure-based screening for prospecting lipases that have structural homolog to Candida antarctica lipase B (CalB). CalB, a widely used biocatalyst, was used as structural template reference because of its enzymatic properties. Structural homolog could aid in th...
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Online Access: | http://dx.doi.org/10.1371/journal.pone.0295397 https://dx.plos.org/10.1371/journal.pone.0295397 |
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crplos:10.1371/journal.pone.0295397 2024-05-19T07:30:50+00:00 Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B Jaito, Nongluck Kaewsawat, Nattha Phetlum, Suthathip Uengwetwanit, Tanaporn Silman, Israel National Science and Technology Development Agency Program Management Unit for Human Resources & Institutional Development, Research and Innovation 2023 http://dx.doi.org/10.1371/journal.pone.0295397 https://dx.plos.org/10.1371/journal.pone.0295397 en eng Public Library of Science (PLoS) http://creativecommons.org/licenses/by/4.0/ PLOS ONE volume 18, issue 12, page e0295397 ISSN 1932-6203 journal-article 2023 crplos https://doi.org/10.1371/journal.pone.0295397 2024-05-01T06:56:41Z Here we employed sequence-based and structure-based screening for prospecting lipases that have structural homolog to Candida antarctica lipase B (CalB). CalB, a widely used biocatalyst, was used as structural template reference because of its enzymatic properties. Structural homolog could aid in the discovery of novel wild-type enzymes with desirable features and serve as a scaffold for further biocatalyst design. The available metagenomic data isolated from various environments was leveraged as a source for bioprospecting. We identified two bacteria lipases that showed high structural similarity to CalB with <40% sequence identity. Partial purification was conducted. In comparison to CalB, the enzymatic characteristics of two potential lipases were examined. A candidate exhibited optimal pH of 8 and temperature of 50°C similar to CalB. The second lipase candidate demonstrated an optimal pH of 8 and a higher optimal temperature of 55°C. Notably, this candidate sustained considerable activity at extreme conditions, maintaining high activity at 70°C or pH 9, contrasting with the diminished activity of CalB under similar conditions. Further comprehensive experimentation is warranted to uncover and exploit these novel enzymatic properties for practical biotechnological purposes. Article in Journal/Newspaper Antarc* Antarctica PLOS PLOS ONE 18 12 e0295397 |
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English |
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Here we employed sequence-based and structure-based screening for prospecting lipases that have structural homolog to Candida antarctica lipase B (CalB). CalB, a widely used biocatalyst, was used as structural template reference because of its enzymatic properties. Structural homolog could aid in the discovery of novel wild-type enzymes with desirable features and serve as a scaffold for further biocatalyst design. The available metagenomic data isolated from various environments was leveraged as a source for bioprospecting. We identified two bacteria lipases that showed high structural similarity to CalB with <40% sequence identity. Partial purification was conducted. In comparison to CalB, the enzymatic characteristics of two potential lipases were examined. A candidate exhibited optimal pH of 8 and temperature of 50°C similar to CalB. The second lipase candidate demonstrated an optimal pH of 8 and a higher optimal temperature of 55°C. Notably, this candidate sustained considerable activity at extreme conditions, maintaining high activity at 70°C or pH 9, contrasting with the diminished activity of CalB under similar conditions. Further comprehensive experimentation is warranted to uncover and exploit these novel enzymatic properties for practical biotechnological purposes. |
author2 |
Silman, Israel National Science and Technology Development Agency Program Management Unit for Human Resources & Institutional Development, Research and Innovation |
format |
Article in Journal/Newspaper |
author |
Jaito, Nongluck Kaewsawat, Nattha Phetlum, Suthathip Uengwetwanit, Tanaporn |
spellingShingle |
Jaito, Nongluck Kaewsawat, Nattha Phetlum, Suthathip Uengwetwanit, Tanaporn Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B |
author_facet |
Jaito, Nongluck Kaewsawat, Nattha Phetlum, Suthathip Uengwetwanit, Tanaporn |
author_sort |
Jaito, Nongluck |
title |
Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B |
title_short |
Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B |
title_full |
Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B |
title_fullStr |
Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B |
title_full_unstemmed |
Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B |
title_sort |
metagenomic discovery of lipases with predicted structural similarity to candida antarctica lipase b |
publisher |
Public Library of Science (PLoS) |
publishDate |
2023 |
url |
http://dx.doi.org/10.1371/journal.pone.0295397 https://dx.plos.org/10.1371/journal.pone.0295397 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
PLOS ONE volume 18, issue 12, page e0295397 ISSN 1932-6203 |
op_rights |
http://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.1371/journal.pone.0295397 |
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PLOS ONE |
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18 |
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12 |
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e0295397 |
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1799467856172154880 |