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Immobilization of penicillin G acylase on macrocellular heterogeneous silica-based monoliths
- Wang, Hua, Jiang, Yanjun, Zhou, Liya, He, Ying, Gao, Jing
- Journal of Molecular Catalysis. B, Enzymatic 2013 v.96 pp. 1-5
- benzylpenicillin, catalytic activity, epoxides, immobilized enzymes, pH, silicon, storage quality, temperature
- A novel material labeled as Si(HIPEs) which possesses macroporosity and mesostructuration was synthesized and functionalized with amino or epoxy groups. The native Si(HIPEs) and functionalized Si(HIPEs) were employed as supports for penicillin G acylase (PGA) immobilization. The effect of pH and temperature on the activity of immobilized PGA was investigated. The reusability, operational stability, storage stability and kinetic properties of the immobilized PGA were examined. Compared with free PGA, the stabilities of immobilized enzyme were improved significantly, especially PGA immobilized on Amino-Si(HIPEs). The excellent reusability of the immobilized PGA will make it useful for potential commercial applications.