Zheng_2025_J.Sci.Food.Agric__

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 lnV(0) = 6.3316 - 4.3321/T, and the activation energy (E(a)) 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 v(max), k(cat), K(m), K(i), and k(cat)/K(m) were 0.01265 micromol L(-1) s(-1), 9310.72 s(-1), 0.4907 mmol L(-1), 3.997 mmol L(-1), and 1.90 x 10(4) 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.