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Amphoteric hydrogels for immobilization of enzymes using template polymerization technique
Author(s) -
ElMasry Mansour M.,
Elnashar Magdy M. M.,
ElSherif Hazem M.
Publication year - 2007
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.26931
Subject(s) - self healing hydrogels , swelling , monomer , polymer chemistry , polymer , polymerization , acrylic acid , methacrylate , immobilized enzyme , chemistry , materials science , chemical engineering , organic chemistry , enzyme , composite material , engineering
Abstract Novel ionizable amphoteric hydrogels were prepared from poly(acrylic acid) and dimethylaminoethyl methacrylate monomer, employing template polymerization technique. The mode of interaction, as proved by FTIR, was multiple H‐bonding between the tertiary amino group of the monomer and the carboxylic groups of the polymer. The impact of varying equal polymer–monomer feed ratios from 0.1 to 1.1 on the swelling dynamics was examined. Penetrant sorption experiments demonstrated that the swelling behavior depends strongly on the polymer complex composition. The polymer complex of feed ratio 0.5 : 0.5 (polymer : monomer) showed maximum swelling percentage. The mechanism of the polymer complexes swelling was probably a non‐Fickian with n values approaching Fickian behavior. The hydrogels showed maximum swelling efficiencies of 27 folds and 13.5 folds in drastic acidic and basic medium, respectively, using polymer complex of 0.5 : 0.5 feed ratio. Because of reversibility and rapidity of swelling, the gel could be considered as a mechanochemical system. The prepared hydrogel successfully immobilized the industrially used β‐galactosidase as an acidic model enzyme. The novel immobilized enzyme showed a remarkable improvement in its activity (13.8 μmol min −1 mg −1 ) compared to the free enzyme (3.2 μmol min −1 mg −1 ). The optimum pH values for free and immobilized enzyme were 4.5–5 and 4, respectively. © 2007 Wiley Periodicals, Inc. J Appl Polym Sci, 2007