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Immobilization of glucose oxidase onto membranes of modified acrylonitrile copolymer
Author(s) -
Godjevargova T. S.,
Dimov A. R.,
Vasileva N.
Publication year - 1994
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.1994.070540309
Subject(s) - acrylonitrile , copolymer , glucose oxidase , glutaraldehyde , hydroxylamine , membrane , polymer chemistry , phase inversion , sodium hydroxide , chemistry , immobilized enzyme , hydroxide , hexamethylenediamine , amine gas treating , diamine oxidase , amine oxidase , organic chemistry , polymer , enzyme , biochemistry , polyamide
Acrylonitrile copolymer was modified with sodium hydroxide and 1,6‐hexamethylen diamine (1) and with hydroxylamine (2). The amount of amine and carboxylic groups was studied as a function of the modification conditions. Membranes were prepared from the modified copolymer by the phase‐inversion method. They were used as matrix for covalent immobilization of glucose oxidase by using glutaraldehyde. The amount of bound protein, relative activity, and storage of the activity fo the immobilized enzyme were determined. The results were compared with those obtained with glucose oxidase immobilized onto the surface‐modified membrane of acrylonitrile copolymer with sodium hydroxide and 1,6‐hexamethylendiamine and with hydroxylamine. The results were proved by scanning electron microscopy. © 1994 John Wiley & Sons, Inc.