Immobilized KDN Lipase on Macroporous Resin for Isopropyl Myristate Synthesis

Abstract

Free enzymes often face economic problems because of their non-repeatability and variability, which limit their application in industrial production. In this study, KDN lipase was immobilized with the macroporous resin LXTE-1000 and glutaraldehyde. The optimal conditions of enzyme immobilization were defined by a single factor experiment and response surface methodology (RSM). The concentration of the cross-linking agent glutaraldehyde was 0.46% (v/v), the cross-linking temperature was 25.0 °C, and the cross-linking time was 157 min. The enzyme activity of the immobilized KDN lipase after adsorption/cross-linking was 291.36 U/g, and the recovery of the enzyme activity was 9.90%. The optimal conditions for the synthesis of isopropyl myristate were catalyzed by the immobilized KDN lipase in a solvent-free system: immobilized enzyme 53 mg, reaction temperature 36.1 °C, myristic acid 228.4 mg, isopropanol 114 µL, and reaction time 18 h. The yield of isopropyl myristate was 66.62%. After ten cycles, the activity of the immobilized KDN lipase preserved more than 46.87% of its initial enzyme activity, and it demonstrated high tolerance to solvents compared to free KDN lipase.

Immobilization of the Lipase B from Candida antarctica on Urban Solid Waste

“…The immobilization of enzymes on stable supports is a tool that allows us to overcome these restrictions. In recent years, various approaches for lipase immobilization have been demonstrated, such as adsorption, encapsulation, cross-linking, and covalent binding [3][4][5][6].…”