Journal of the science of food and agriculture · 2025
Selective synthesis of triacylglycerols by the ADS-17-supported Candida antarctica lipase B through esterification of oleic acid and glycerol.
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Zheng Jiawei, Zhang Qiangyue, Zhong Nanjing
Аннотация
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.
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.