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Immobilization studies of an industrial penicillin acylase preparation on a silica carrier
Author(s) -
Fonseca L. P.,
Cardoso J. P.,
Cabral J. M. S.
Publication year - 1993
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.280580105
Subject(s) - glutaraldehyde , immobilized enzyme , silanization , chemistry , hydrolysis , covalent bond , penicillin amidase , chromatography , penicillin , covalent binding , silica gel , organic chemistry , enzyme , biochemistry , antibiotics
Penicillin acylase (EC 3.5.1.11) was immobilized by covalent binding on a silica gel carrier activated by silanization. High immobilization yields, operational stability, enzyme loading and support reutilization capacity were obtained. The effects of several variables on the activation of the support and on the immobilization method were studied. Other supports and immobilization methods were assessed for the immobilization of penicillin acylase and compared with the basic process used. Activity versus temperature, pH, buffer molarity and penicillin concentration profiles were determined and compared for the free, crosslinked and covalently‐bound silica carrier penicillin acylase preparations. The hydrolysis performance of the latter preparation was assessed in a batch basket reactor and the time course of the hydrolysis reaction modelled by a two parameter model equation. The operational stabilities of penicillin acylase coupled covalently to the silica gel support and immobilized by a crosslinking procedure using glutaraldehyde were also compared.