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https://doi.org/10.3390/ijms221910339
Title: | A Novel Lipase from Lasiodiplodia theobromae Efficiently Hydrolyses C8-C10 Methyl Esters for the Preparation of Medium-Chain Triglycerides' Precursors | Authors: | Ng, Andre Mong Jie Yang, Renliang Zhang, Hongfang Xue, Bo Yew, Wen Shan Nguyen, Giang Kien Truc |
Keywords: | Science & Technology Life Sciences & Biomedicine Physical Sciences Biochemistry & Molecular Biology Chemistry, Multidisciplinary Chemistry enzyme discovery lipase medium-chain triglycerides methyl esters sustainability zymogram CANDIDA-ANTARCTICA TRIACYLGLYCEROLS DALI |
Issue Date: | 1-Oct-2021 | Publisher: | MDPI | Citation: | Ng, Andre Mong Jie, Yang, Renliang, Zhang, Hongfang, Xue, Bo, Yew, Wen Shan, Nguyen, Giang Kien Truc (2021-10-01). A Novel Lipase from Lasiodiplodia theobromae Efficiently Hydrolyses C8-C10 Methyl Esters for the Preparation of Medium-Chain Triglycerides' Precursors. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 22 (19). ScholarBank@NUS Repository. https://doi.org/10.3390/ijms221910339 | Abstract: | Medium-chain triglycerides (MCTs) are an emerging choice to treat neurodegenerative disorders such as Alzheimer’s disease. They are triesters of glycerol and three medium-chain fatty acids, such as capric (C8) and caprylic (C10) acids. The availability of C8–C10 methyl esters (C8– C10 ME) from vegetable oil processes has presented an opportunity to use methyl esters as raw materials for the synthesis of MCTs. However, there are few reports on enzymes that can efficiently hydrolyse C8–C10 ME to industrial specifications. Here, we report the discovery and identification of a novel lipase from Lasiodiplodia theobromae fungus (LTL1), which hydrolyses C8–C10 ME effi-ciently. LTL1 can perform hydrolysis over pH ranges from 3.0 to 9.0 and maintain thermotolerance up to 70 °C. It has high selectivity for monoesters over triesters and displays higher activity over commercially available lipases for C8–C10 ME to achieve 96.17% hydrolysis within 31 h. Structural analysis by protein X-ray crystallography revealed LTL1′s well-conserved lipase core domain, to-gether with a partially resolved N-terminal subdomain and an inserted loop, which may suggest its hydrolytic preference for monoesters. In conclusion, our results suggest that LTL1 provides a trac-table route towards to production of C8–C10 fatty acids from methyl esters for the synthesis of MCTs. | Source Title: | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | URI: | https://scholarbank.nus.edu.sg/handle/10635/218738 | ISSN: | 16616596 14220067 |
DOI: | 10.3390/ijms221910339 |
Appears in Collections: | Staff Publications Elements |
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