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A Novel Lipase from Lasiodiplodia theobromae Efficiently Hydrolyses C8-C10 Methyl Esters for the Preparation of Medium-Chain Triglycerides' Precursors.
Ng, Andre Mong Jie; Yang, Renliang; Zhang, Hongfang; Xue, Bo; Yew, Wen Shan; Nguyen, Giang Kien Truc.
Afiliação
  • Ng AMJ; WIL@NUS Corporate Laboratory, Wilmar International Limited, Centre for Translational Medicine, 14 Medical Drive, Singapore 117599, Singapore.
  • Yang R; Wilmar Innovation Centre, Wilmar International Limited, 28 Biopolis Road, Singapore 138568, Singapore.
  • Zhang H; Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, 8 Medical Drive, Singapore 117596, Singapore.
  • Xue B; NUS Synthetic Biology for Clinical and Technological Innovation, Centre for Life Sciences, National University of Singapore, 28 Medical Drive, Singapore 117456, Singapore.
  • Yew WS; NUS Synthetic Biology Translational Research Programme, Centre for Translational Medicine, National University of Singapore, 14 Medical Drive, Singapore 117599, Singapore.
  • Nguyen GKT; WIL@NUS Corporate Laboratory, Wilmar International Limited, Centre for Translational Medicine, 14 Medical Drive, Singapore 117599, Singapore.
Int J Mol Sci ; 22(19)2021 Sep 25.
Article em En | MEDLINE | ID: mdl-34638680
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 efficiently. 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, together 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 tractable route towards to production of C8-C10 fatty acids from methyl esters for the synthesis of MCTs.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ascomicetos / Ésteres / Lipase Idioma: En Revista: Int J Mol Sci Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Singapura

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ascomicetos / Ésteres / Lipase Idioma: En Revista: Int J Mol Sci Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Singapura