Enregistré dans:
| Auteurs principaux: | , , , , , , , , , |
|---|---|
| Format: | Artículo científico |
| Langue: | en |
| Publié: |
International journal of biological macromolecules
2026
|
| Accès en ligne: | https://pubmed.ncbi.nlm.nih.gov/42251877/ |
| Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
| _version_ | 1868266039407542274 |
|---|---|
| author | Tian, Tian Jiang, Lijia Zhao, Dongfeng Yu, Hao Jiang, Lingbo Wang, Jian Shuai, Yiying Ma, Zhongjun Li, Yanhong Zhang, Chunfang |
| author_facet | Tian, Tian Jiang, Lijia Zhao, Dongfeng Yu, Hao Jiang, Lingbo Wang, Jian Shuai, Yiying Ma, Zhongjun Li, Yanhong Zhang, Chunfang Tian, Tian Jiang, Lijia Zhao, Dongfeng Yu, Hao Jiang, Lingbo Wang, Jian Shuai, Yiying Ma, Zhongjun Li, Yanhong Zhang, Chunfang |
| collection | PubMed - marine biology |
| contents | Medium-chain substrate preference of lipases from a novel deep-sea halotolerant bacterium revealed by enzymatic assays and molecular docking. Tian, Tian Jiang, Lijia Zhao, Dongfeng Yu, Hao Jiang, Lingbo Wang, Jian Shuai, Yiying Ma, Zhongjun Li, Yanhong Zhang, Chunfang Lipases from halotolerant bacteria represent promising biocatalysts for industrial applications due to their stability under extreme conditions. In this study, a halotolerant strain Salegentibacter sp. MHS1-6 was isolated from Western Pacific deep-sea sediments, and its lipase was characterized for the first time. The crude enzyme was first precipitated with 60% ammonium sulfate and then purified by Superdex 200 Increase. The final purified enzyme exhibited a specific activity of 187.4 ± 11.8 U/mg and a recovery yield of 24.7 ± 1.8%. Enzymatic characterization showed that the lipase retained high activity in 4.5 mol/L NaCl and at pH 11, revealing substantial tolerance to combined salinity and alkaline stress. Substrate specificity analysis showed a distinct preference for medium-chain substrates, including tricaprylin and p-nitrophenyl caprylate. Molecular docking provided preliminary insights into the potential structural basis of this chain-length preference, suggesting that C8-C10 acyl chains may form relatively favorable hydrogen-bonding and hydrophobic contacts within the catalytic pocket. This work presents the first detailed characterization of a deep-sea lipase, highlighting its potential for biocatalysis in high-salt and alkaline environments. While the precise catalytic mechanism requires further validation, its robust properties make it a promising candidate for industrial processes that demand exceptional stability. |
| format | Artículo científico |
| id | pubmed_42251877 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | International journal of biological macromolecules |
| record_format | pubmed |
| spellingShingle | Medium-chain substrate preference of lipases from a novel deep-sea halotolerant bacterium revealed by enzymatic assays and molecular docking. Tian, Tian Jiang, Lijia Zhao, Dongfeng Yu, Hao Jiang, Lingbo Wang, Jian Shuai, Yiying Ma, Zhongjun Li, Yanhong Zhang, Chunfang Medium-chain substrate preference of lipases from a novel deep-sea halotolerant bacterium revealed by enzymatic assays and molecular docking. Tian, Tian Jiang, Lijia Zhao, Dongfeng Yu, Hao Jiang, Lingbo Wang, Jian Shuai, Yiying Ma, Zhongjun Li, Yanhong Zhang, Chunfang Lipases from halotolerant bacteria represent promising biocatalysts for industrial applications due to their stability under extreme conditions. In this study, a halotolerant strain Salegentibacter sp. MHS1-6 was isolated from Western Pacific deep-sea sediments, and its lipase was characterized for the first time. The crude enzyme was first precipitated with 60% ammonium sulfate and then purified by Superdex 200 Increase. The final purified enzyme exhibited a specific activity of 187.4 ± 11.8 U/mg and a recovery yield of 24.7 ± 1.8%. Enzymatic characterization showed that the lipase retained high activity in 4.5 mol/L NaCl and at pH 11, revealing substantial tolerance to combined salinity and alkaline stress. Substrate specificity analysis showed a distinct preference for medium-chain substrates, including tricaprylin and p-nitrophenyl caprylate. Molecular docking provided preliminary insights into the potential structural basis of this chain-length preference, suggesting that C8-C10 acyl chains may form relatively favorable hydrogen-bonding and hydrophobic contacts within the catalytic pocket. This work presents the first detailed characterization of a deep-sea lipase, highlighting its potential for biocatalysis in high-salt and alkaline environments. While the precise catalytic mechanism requires further validation, its robust properties make it a promising candidate for industrial processes that demand exceptional stability. |
| title | Medium-chain substrate preference of lipases from a novel deep-sea halotolerant bacterium revealed by enzymatic assays and molecular docking. |
| url | https://pubmed.ncbi.nlm.nih.gov/42251877/ |