Zou_2025_Food.Chem_474_143151

Reference

Title : Lipase-catalyzed esterification for efficient acylglycerols synthesis in a solvent-free system: Process optimization, mass transfer insights and kinetic modeling - Zou_2025_Food.Chem_474_143151
Author(s) : Zou S , Zhang Z , Lee YY , Ai H , Zhang Y , Wang Y
Ref : Food Chem , 474 :143151 , 2025
Abstract :

Acylglycerols are widely used in the food industry due to their antimicrobial, emulsifying and nutritional properties. This study investigated the key reaction parameters, mass transfer mechanisms, and kinetic features of lipase-catalyzed esterification in a solvent-free system. Taguchi method was further employed to explore the relationship between "reaction parameter - yield composition". The results revealed that the maximum selectivity were achieved fror MAG (57.72 %), DAG (82.67 %) and TAG (79.29 %) under different enzymatic conditions. Fatty acid-to-glycerol molar ratio had the greatest impact on DAG selectivity, contributing 38.08 % of total impact level. Mass transfer analysis showed that external mass transfer limitation could be effectively overcome at stirring speeds above 600 rpm. Kinetic analysis confirmed that the reaction followed the Ping-Pong BiBi mechanism with alcohol and acid inhibition (SSE = 0.000643). This work provided a theoretical basis for developing more efficient and selective catalytic processes, aiding in quality control, reactor design, and industrial scale-up.

PubMedSearch : Zou_2025_Food.Chem_474_143151
PubMedID: 39891972

Related information

Citations formats

Zou S, Zhang Z, Lee YY, Ai H, Zhang Y, Wang Y (2025)
Lipase-catalyzed esterification for efficient acylglycerols synthesis in a solvent-free system: Process optimization, mass transfer insights and kinetic modeling
Food Chem 474 :143151

Zou S, Zhang Z, Lee YY, Ai H, Zhang Y, Wang Y (2025)
Food Chem 474 :143151