IMMOBILIZATION STUDIES OF PENICILLIN ACYLASE ON THE POROUS BEAD WITH OXIRANE GROUPS / 微生物学通报

ABSTRACT

Penicillin Acylase from B. megaterium was immobilized on the porous bead carriers based on methacrylate, N,N-methelene-bis-methacrymide, glycidyl methacrylate, Allyl ether copolymers (Eupergit-c) either directly or after chemical modification with 1.6-deaminohexane and L-Lysine. Directly binding with oxirane groups, the most efficient immobilization results were achieved. The immobilization yield was markedly influenced by the ratio of amount of free enzyme to the weight of the carrier. The specific activities of 89 up to 475IU/g (wet) and binding protein of 6.9 to 112 mg/g (dry) were obtained when the free enzyme added to the immobilization solution was from 323IU/g (dry) up to 6250IU/g (dry). The residual activity of immobilized PGA in a recycling system at the 20th was about 92.5% of the initial value.