Abstract
AbstractThis work reported a novel immobilization method of penicillin acylase (PA) using nucleophilic substitution reaction between benzyl chloride on macroporous adsorption resin (MAR) and amino groups on PA. Nucleophilic substitution reaction of benzyl chloride was reported for the first time in enzyme immobilization. The work was conducted as follows: Firstly, an apolar MAR, LX1180, was chemically modified, that is, chloromethylated, to prepare benzyl chloride LX1180 (CLX1180). Then, CLX1180 was used as a support to immobilize PA through nucleophilic substitution. The influence of reaction conditions, such as immobilization time, temperature, pH, and the amount of PA, on the loading ratio and catalytic activity were investigated and optimized. Besides, this study indicated that the immobilization reaction was a diffusion‐controlled reaction. Finally, the structure of immobilized PA was characterized using FTIR, and the stability for catalyst activity was explored by investigating the reusability of the sample, and the result indicated that PA was immobilized on the surface of CLX1180 successfully and presented an excellent stability of catalyst activity. It proposed a simple and promising way to immobilize PA for enzyme catalysis.
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