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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| Format: | Article |
| Language: | English |
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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 |
| _version_ | 1797377758432591872 |
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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. |
| first_indexed | 2024-03-08T19:57:07Z |
| format | Article |
| id | doaj.art-68128c2beee0475a84a4f74136dc2316 |
| 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) |
| record_format | Article |
| series | PLoS ONE |
| 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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