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Properties of penicillin amidase immobilized by copolymerization with acrylamide
Author(s) -
Szewczuk Apolinary,
Ziomek Edmund,
Mordarski Marian,
Siewiński Maciej,
Wieczorek Jadwiga
Publication year - 1979
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260210904
Subject(s) - amidase , penicillin amidase , benzylpenicillin , acrylamide , copolymer , chemistry , phenylacetate , maleic anhydride , substrate specificity , substrate (aquarium) , penicillin , enzyme , polymer chemistry , immobilized enzyme , chromatography , biochemistry , organic chemistry , polymer , antibiotics , biology , ecology
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 enyme, 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.