Production and immobilization of lipase PCL and its application in synthesis of α‐linolenic acid‐rich diacylglycerol

This study examined the production, immobilization of lipase PCL, and its application in the synthesis of diacylglycerol by esterification of α‐linolenic acid with glycerol. The resin ECR880 6 was selected as an effective support for the immobilization of lipase PCL. Fourier transform infrared and Laser scanning confocal microscope analysis proved that the lipase was successfully immobilized on the resin. Compared with the free PCL, the immobilized one exhibited higher temperature toler ance. Under optimized reaction conditions, a DAG content of 54.49% were obtained. After further purified by molecular distillation, the purity of DAG was up to 99.28%. During esterification, the immobilized PCL was quite stable and retained more than 91.60% of its initial activity after 10 cycles. T hese new findings on the immobilized PCL will make it to be a prospective enzyme in oils and fats industry.Practical applicationsImmobilized PCL, a monoacylglycerol and diacylglycerol lipase, was first employed to synthesis of a high purity α‐linolenic acid‐rich diacylglycerol. The improved biocatalytic performance and reusability of the lipase make it to be a promising catalyst in industrial application.

Source: Journal of Food Biochemistry - October 24, 2018 Category: Food Science Authors: Nan Liu, Daoming Li, Weifei Wang, Frank Hollmann, Long Xu, Yunjian Ma, Bo Yang, Weidong Bai, Xiaotao Sun, Yonghua Wang Tags: FULL ARTICLE Source Type: research