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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ftdoajarticles:oai:doaj.org/article:68128c2beee0475a84a4f74136dc2316 2024-01-28T09:58:49+01:00 Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B. Nongluck Jaito Nattha Kaewsawat Suthathip Phetlum Tanaporn Uengwetwanit 2023-01-01T00:00:00Z https://doi.org/10.1371/journal.pone.0295397 https://doaj.org/article/68128c2beee0475a84a4f74136dc2316 EN eng Public Library of Science (PLoS) https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0295397&type=printable https://doaj.org/toc/1932-6203 1932-6203 doi:10.1371/journal.pone.0295397 https://doaj.org/article/68128c2beee0475a84a4f74136dc2316 PLoS ONE, Vol 18, Iss 12, p e0295397 (2023) Medicine R Science Q article 2023 ftdoajarticles https://doi.org/10.1371/journal.pone.0295397 2023-12-31T01:49:22Z 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 Directory of Open Access Journals: DOAJ Articles PLOS ONE 18 12 e0295397 |
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language |
English |
topic |
Medicine R Science Q |
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Medicine R Science Q Nongluck Jaito Nattha Kaewsawat Suthathip Phetlum Tanaporn Uengwetwanit Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B. |
topic_facet |
Medicine R Science Q |
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. |
format |
Article in Journal/Newspaper |
author |
Nongluck Jaito Nattha Kaewsawat Suthathip Phetlum Tanaporn Uengwetwanit |
author_facet |
Nongluck Jaito Nattha Kaewsawat Suthathip Phetlum Tanaporn Uengwetwanit |
author_sort |
Nongluck Jaito |
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 |
https://doi.org/10.1371/journal.pone.0295397 https://doaj.org/article/68128c2beee0475a84a4f74136dc2316 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
PLoS ONE, Vol 18, Iss 12, p e0295397 (2023) |
op_relation |
https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0295397&type=printable https://doaj.org/toc/1932-6203 1932-6203 doi:10.1371/journal.pone.0295397 https://doaj.org/article/68128c2beee0475a84a4f74136dc2316 |
op_doi |
https://doi.org/10.1371/journal.pone.0295397 |
container_title |
PLOS ONE |
container_volume |
18 |
container_issue |
12 |
container_start_page |
e0295397 |
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1789330465213120512 |