Li_2024_Int.J.Biol.Macromol__136356

The stability of the immobilized lipase is the key factor that determines the economy and feasibility of its industrial application. Here, two robust immobilized Candida antarctica lipase B (CALB) were prepared through adjusting the surface properties of ECR1030 resin. Silane coupling agent (SCA) and dialdehyde cellulose (DAC) were employed to modify the carrier surface. Contact angle measurement showed that the hydrophobicity of the modified carrier increased first, and then decreased with the increase of the chain length of SCA. FTIR results showed that Si-O-Si bond and aldehyde group were attached to ECR1030, respectively, indicating that the ECR1030 resin was successfully modified. Meanwhile, the NH and CN bond were observed in the corresponding immobilized CALB, suggesting CALB was immobilized onto the modified carriers. The effects of immobilization conditions on CALB immobilization was further investigated, and the C(8)-ECR1030-CALB and DAC-ECR1030-CALB with the activity of 12,736 U/g and 11,962 U/g were obtained. Moreover, the stability of the immobilized lipases was evaluated and compared with the commercial Novozym 435. The C(8)-ECR1030-CALB and DAC-ECR1030-CALB exhibited comparable or superior stability to Novozym 435 and showed better deacidification effect than Novozym 435. This study paves road for further study involving preparation of highly stable immobilized lipase.