Interface-based kinetic model considering the integral stereoselectivity of lipases on tricapryloylglycerol in a reverse micelle system

Food Chem. 2025 Feb 15;465(Pt 1):141403. doi: 10.1016/j.foodchem.2024.141403. Epub 2024 Sep 23.

Abstract

Lipases are essential enzymes with unique selectivity, making them valuable in industrial applications. Understanding the integral stereoselectivity of lipases during triacylglycerol (TAG) hydrolysis is crucial for producing high-value products, such as structured lipids. This study developed an analytical method and an interface-based kinetic model to determine integral stereoselectivities on tricapryloylglycerol (TCG), a medium-chain TAG. The analytical method used an HPLC system that simultaneously separated TCG and its hydrolysates with resolution factors of >2.4 and relative standard deviation of retention times <0.3 % within 15 min. The interface-based kinetic model was established to determine the integral stereoselectivities according to the characteristics of the reaction system. The model provided better fitting results for TCG and trioleoylglycerol hydrolysis than a previous model, indicating the successful application in both medium- and long-chain TAGs. This study expanded our understanding of integral stereoselectivity and could facilitate the development of various structured lipid syntheses.

Keywords: Chiral stationary phase column; Integral stereoselectivity; Interface-based kinetic model; Lipase; Medium-chain triacylglycerol.

MeSH terms

  • Biocatalysis
  • Enzymes, Immobilized / chemistry
  • Enzymes, Immobilized / metabolism
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism
  • Hydrolysis
  • Kinetics
  • Lipase* / chemistry
  • Lipase* / metabolism
  • Micelles*
  • Stereoisomerism
  • Substrate Specificity
  • Triglycerides* / chemistry
  • Triglycerides* / metabolism

Substances

  • Lipase
  • Triglycerides
  • Micelles
  • Fungal Proteins
  • Enzymes, Immobilized