The demand for infant formula similar to breast milk is growing.To address this,this study investigated the catalytic preparation of 1-oleic acid-2-palmitic acid-3-linoleic acid triglyceride(OPL),the main lipid component in human milk,using a new immobilized lipase,ANL-MARE.The immobilized lipase ANL-MARE was successfully prepared and characterized.Next,an efficient enzyme-catalyzed preparation of lipids rich in OPL structures from tripalmitin,oleic acid,and linoleic acid was established using ANL-MARE as the biocatalyst.After optimization via single-factor and response surface experiments,the optimal OPL synthesis process was obtained,with the following characteristics:a tripalmitin:total fatty acids molar ratio of 1∶14.27;an oleic acid:linoleic acid molar ratio of 1∶0.76;the addition of 12.70%ANL-MARE;a reaction temperature of 50℃,and a reaction time of 4 h.Under these conditions,the relative OPL content reached 47.93%,and sn-2 palmitic acid accounted for 71.69%of the total palmitic acid content(reflecting the relative sn-2 palmitic acid content).In addition,the immobilized lipase ANL-MARE showed better catalytic activity than commercial lipases in OPL synthesis.In conclusion,the immobilized lipase ANL-MARE has significant potential to catalyze the preparation of lipids with OPL structures.This study provides a novel strategical and theoretical basis for the efficient preparation of human milk fat substitutes.
维普
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