Please use this identifier to cite or link to this item: https://doi.org/10.3390/ijms221910339
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dc.titleA Novel Lipase from Lasiodiplodia theobromae Efficiently Hydrolyses C8-C10 Methyl Esters for the Preparation of Medium-Chain Triglycerides' Precursors
dc.contributor.authorNg, Andre Mong Jie
dc.contributor.authorYang, Renliang
dc.contributor.authorZhang, Hongfang
dc.contributor.authorXue, Bo
dc.contributor.authorYew, Wen Shan
dc.contributor.authorNguyen, Giang Kien Truc
dc.date.accessioned2022-04-08T07:00:49Z
dc.date.available2022-04-08T07:00:49Z
dc.date.issued2021-10-01
dc.identifier.citationNg, 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
dc.identifier.issn16616596
dc.identifier.issn14220067
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/218738
dc.description.abstractMedium-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.
dc.language.isoen
dc.publisherMDPI
dc.sourceElements
dc.subjectScience & Technology
dc.subjectLife Sciences & Biomedicine
dc.subjectPhysical Sciences
dc.subjectBiochemistry & Molecular Biology
dc.subjectChemistry, Multidisciplinary
dc.subjectChemistry
dc.subjectenzyme discovery
dc.subjectlipase
dc.subjectmedium-chain triglycerides
dc.subjectmethyl esters
dc.subjectsustainability
dc.subjectzymogram
dc.subjectCANDIDA-ANTARCTICA
dc.subjectTRIACYLGLYCEROLS
dc.subjectDALI
dc.typeArticle
dc.date.updated2022-04-07T04:02:26Z
dc.contributor.departmentBIOCHEMISTRY
dc.contributor.departmentLIFE SCIENCES INSTITUTE
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.description.doi10.3390/ijms221910339
dc.description.sourcetitleINTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
dc.description.volume22
dc.description.issue19
dc.published.statePublished
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