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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Public Library of Science (PLoS)
2023-01-01
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Series: | PLoS ONE |
Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0295397&type=printable |
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author | Nongluck Jaito Nattha Kaewsawat Suthathip Phetlum Tanaporn Uengwetwanit |
author_facet | Nongluck Jaito Nattha Kaewsawat Suthathip Phetlum Tanaporn Uengwetwanit |
author_sort | Nongluck Jaito |
collection | DOAJ |
description | 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. |
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institution | Directory Open Access Journal |
issn | 1932-6203 |
language | English |
last_indexed | 2024-03-08T19:57:07Z |
publishDate | 2023-01-01 |
publisher | Public Library of Science (PLoS) |
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spelling | doaj.art-68128c2beee0475a84a4f74136dc23162023-12-24T05:33:28ZengPublic Library of Science (PLoS)PLoS ONE1932-62032023-01-011812e029539710.1371/journal.pone.0295397Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B.Nongluck JaitoNattha KaewsawatSuthathip PhetlumTanaporn UengwetwanitHere 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.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0295397&type=printable |
spellingShingle | Nongluck Jaito Nattha Kaewsawat Suthathip Phetlum Tanaporn Uengwetwanit Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B. PLoS ONE |
title | 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_short | 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 |
url | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0295397&type=printable |
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