Immobilization of Candida antarctica Lipase B Onto ECR1030 Resin and its Application in the Synthesis of n‐3 PUFA‐Rich Triacylglycerols

In this study, Candida antarctica lipase B (CALB) is immobilized onto ECR1030 resin and the obtained immobilized preparation is used for the synthesis of n‐3 polyunsaturated fatty acids (PUFA)‐rich triacylglycerols (TAG). The immobilization process is systematically studied. Under the optimized conditions, the immobilized preparation of ECR1030‐CALB with an esterification activity of 10 058 U g −1 is obtained, which is comparable with the commercially available Novozym 435. Confocal microscopy images showed that CALB diffused from the surface to the center of carrier during immobilization. The basic properties of ECR1030‐CALB is also investigated and it is found that the thermostability, acidic and alkaline stability, and organic solvent tolerance of ECR1030‐CALB are comparable with Novozym 435. Interestingly, ECR1030‐CALB showed significantly higher specificity toward EPA and DHA compared with Novozym 435, which made it suitable for the synthesis of n‐3 PUFA‐rich TAG. Overall, the prepared ECR1030‐CALB with excellent esterification activity, basic properties, and catalytic performance might be a promising alternative to commercial Novozym 435. Practical Applications : A previous study found that ECR1030 resin was a robust and promising carrier for the immobilization of CALB. However, the detailed immobilization conditions, the basic properties, and catalytic performance of the immobilized preparations using ECR1030 resin as carrier are still unknown. Consequently, knowledge of the above unknown information for the immobilization of CALB using ECR1030 resin as carrier is of great importance for their further practical applications in lipid chemistry.