Lipase/Esterase: Properties and industrial applications

Oi Ming Lai, Yee Ying Lee, Eng Tong Phuah, Casimir C. Akoh

    Research output: Chapter in Book/Report/Conference proceedingEncyclopaedia / Dictionary EntryOtherpeer-review

    12 Citations (Scopus)

    Abstract

    Lipases and esterases are both versatile biocatalysts that catalyse and accelerate the hydrolysis of ester-linked compounds. Lipases preferentially catalyse hydrolysis of water-insoluble esters such as triacylglycerols (TAGs) whereas esterases hydrolyse water-soluble esters or short-chain fatty acid TAG. Their high selectivity with broad substrate range makes these biocatalysts an ideal catalyst for organic synthesis in comparison to conventional chemical catalysts. The present monograph covers topics such as the original sources and classification of lipases and esterases, their respective catalytic properties as well as their substrate selectivity. Moreover, the potential applications of these enzymes with reference to food, cosmetic and pharmaceutical industries in recent years are discussed extensively in this article.

    Original languageEnglish
    Title of host publicationEncyclopedia of Food Chemistry
    EditorsLaurence Melton, Fereidoon Shahidi, Peter Varelis
    PublisherElsevier
    Chapter20
    Pages158-167
    Number of pages10
    Volume2
    ISBN (Electronic)9780128140451
    ISBN (Print)9780128140260
    DOIs
    Publication statusPublished - 2019

    Keywords

    • Chiral drug
    • Cholesterol esterase
    • Cutinase
    • Emulsifier
    • Enantioselectivity
    • Esterase
    • Feruloyl esterase
    • Flavouring
    • Human milk fat substitute
    • Hydroxycinnamic acid
    • Lipase
    • Phospholipase
    • Phytosterol
    • Structured lipid
    • Sugar fatty acid ester

    Cite this