One-dimensional cross-linked enzyme aggregate strategy for penicillin acylase immobilization in mesopores

In order to improve the stability of penicillin acylase (PA), the strategy of one-dimensional cross-linked enzyme aggregate (CLEA) was introduced to the immobilization process of PA. Mesocellular siliceous foams (MCFs) with large pore diameter were synthesized, and PA was coupled to MCFs through adsorption and covalent linkage by benzoquinine. The experimental results show that the stability of PA is greatly increased, and the optimal temperature of PA is increased from 45°C to 55°C. After thermal treatment at 50°C for 25 h, the activity of immobilized enzyme remains 74.4%, maintaining 61.9% activity after repeated use for 15 times.