Immobilized lipase, as a hot research field of enzyme engineering, can effectively overcome the shortcomings of natural enzymes such as unstable, easy to inactivate and difficult to reuse. In this paper, chitosan microspheres were prepared from chitosan and modified with succinic anhydride to obtain a series of N-succinyl chitosan with different degrees of substitution. The N-succinyl chitosan microspheres were used as carriers, and the microspheres were fully solubilized and immobilized with lipase by the embedding method. The effects of pH and cross-linking temperature on the immobilized enzyme activity were explored to determine the optimal experimental environmental parameters. Hydrolysis experiments were designed to characterize the biocatalytic efficacy of lipase for hydrolysis of long-chain fatty acid ester pollutants using olive oil. The optimal reaction pH and the optimal cross-linking temperature for the immobilized lipase were measured to be 7.5 pH and 48 °C, respectively. After catalytic hydrolysis for 40 min, the degradation efficiency of the immobilized lipase for long-chain fatty acid ester pollutants reached about 1.6 times that of the free lipase, with an efficiency as high as 70.12%.
