Please use this identifier to cite or link to this item: 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
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