Amphoteric hydrogels for immobilization of enzymes using template polymerization technique

• Published in: Journal of applied polymer science 2007-12, Vol.106 (6), p.3571-3580
• Main Authors: El-Masry, Mansour M, Elnashar, Magdy M.M, El-Sherif, Hazem M
• Format: Article
• Language: English
• Subjects: amphoteric hydrogels; Applied sciences; Biological and medical sciences; Biotechnology; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; Immobilization of enzymes and other molecules; Immobilization techniques; Methods. Procedures. Technologies; non-Fickian mechanism; Organic polymers; Physicochemistry of polymers; polyacrylic acid; Properties and characterization; Solution and gel properties; template polymerization; β-galactosidase immobilization
• ISSN: 0021-8995; 1097-4628
• DOI: 10.1002/app.26931

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