Understanding the integral stereoselectivity of Cordyceps militaris lipase for medium-chain triglycerides: Tricaprylin-based kinetic and molecular docking analysis.

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Citation abstract

Medium-chain triglycerides (MCTs) have garnered considerable attention in the food and health industries due to their rapid absorption, efficient metabolism, and nutritional benefits compared to long-chain triglycerides. In this study, the integral stereoselectivities of both native and recombinant forms of an MCT-selective lipase, Cordyceps militaris lipase (CML), toward tricaprylin (TC) were determined to evaluate their potential applications to MCTs. Lipase assays revealed that catalytic activities were markedly enhanced in the presence of 30 mM sodium cholate, with 6.9-fold and 1.9-fold increases for native and recombinant CML, respectively. To accurately monitor hydrolysis of TC, an optimized HPLC system was established, enabling efficient separation and quantification of TC and its hydrolysates. Kinetic modeling indicated that native and recombinant CML showed a preference for the sn-3 position over all other sn positions of TC by 98% and 70%, respectively. To further validate these findings, covalent docking of TC into CML, which mimics its tetrahedral intermediate, was simulated, confirming the sn-3 selectivity of CML to TC. Overall results indicated the industrial potential of CML as a biocatalyst for producing structured lipids, such as low-calorie lipids, from MCTs, highlighting its potential application in food processing.