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

22 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

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