Selective synthesis of triacylglycerols by the ADS‐17‐supported Candida antarctica lipase B through esterification of oleic acid and glycerol.

BACKGROUND: Immobilized enzyme possessing both high activity and good selectivity is important in practice. In this study, Candida antarctica lipase B (CALB) was immobilized onto the macroporous resin ADS‐17 for triacylglycerol (TAG) synthesis through esterification of oleic acid and glycerol. The reaction conditions were optimized by single‐factor study and orthogonal test, and the reusability of the immobilized CALB (CALB@ADS‐17) was evaluated. In addition, the mechanism of lipase immobilization was studied and the catalytic mechanism of CALB@ADS‐17 was investigated. RESULTS: Oleic acid conversion up to 99.20% and TAG content at 91.58 wt% could be obtained under optimal conditions. In addition, the CALB@ADS‐17 retained 84.28% of its initial activity after 11 cycles of reuse. The mechanism of lipase immobilization was through hydrophobic adsorption. The relationship between temperature and oleic acid conversion was lnV0 = 6.3316 − 4.3321/T, and the activation energy (Ea) was 36.02 kJ mol−1. CALB@ADS‐17 did not exhibit an obvious interfacial activation phenomenon. Its kinetic behavior can be described by the Michaelis–Menten model, whose kinetic parameters of vmax, kcat, Km, Ki, and kcat/Km were 0.01265 μmol L−1 s−1, 9310.72 s−1, 0.4907 mmol L−1, 3.997 mmol L−1, and 1.90 × 104 L mmol−1 s−1, respectively. CONCLUSION: CALB@ADS‐17 showed good esterification performance and exhibited good selectivity towards TAG generation. In addition, CALB@ADS‐17 exhibited good reusability in esterification reactions and has potential in practical applications. © 2025 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]