Synthesis of 1-Oleic Acid-2-Palmitic Acid-3-Linoleic Acid Triglyceride via Enzymatic Acidolysis by Immobilized Lipase ANL-MARE
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Abstract:
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.
