Properties of penicillin amidase immobilized by copolymerization with acrylamide.
An enzyme preparation in a spherical granule form was obtained by copolymerization of penicillin amidase (EC 3.5.1.11) (previously modified with maleic anhydride) and acrylamide via a crosslinking agent. As compared with the native enzyme, immobilized amidase is more resistant to heating, has a lower affinity to benzylpenicillin, and is less inhibited by phenylacetate. Its substrate specificity and optimum pH remain unchanged.
D000178:Acrylamides; D000581:Amidohydrolases / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D005029:Ethylenediamines; D005782:Gels; D008299:Maleic Anhydrides / Q000494:pharmacology; D010399:Penicillin Amidase / Q000378:metabolism*; D010400:Penicillin G / Q000378:metabolism; D011108:Polymers
D000178:Acrylamides; D004800:Enzymes, Immobilized; D005029:Ethylenediamines; D005782:Gels; D008299:Maleic Anhydrides; D011108:Polymers; D000581:Amidohydrolases; D010399:Penicillin Amidase; D010400:Penicillin G