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Immobilization of catalase on a novel polymer support, crosslinked polystyrene ethylene glycol acrylate resin: Role of the macromolecular matrix on enzyme activity
Author(s) -
Kumar G. S. Vinod,
Kumar K. Santhosh
Publication year - 2005
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.21666
Subject(s) - ethylene glycol , polystyrene , polymer chemistry , ethylene glycol dimethacrylate , acrylate , styrene , materials science , polymer , ethylene , chemistry , catalysis , copolymer , organic chemistry , methacrylic acid
Crosslinked polystyrene ethylene glycol acrylate resin (CLPSER) was developed for the immobilization of the enzyme catalase by the introduction of a crosslinker, O , O ′‐bis(2‐acrylamidopropyl) poly(ethylene glycol) 1900 , to styrene. The crosslinker was prepared by the treatment of acryloyl chloride with O , O ′‐bis(2‐aminopropyl) poly(ethylene glycol) 1900 in the presence of diisopropylethylamine. The resin was characterized with IR and 13 C‐NMR spectroscopy. The catalytic activity of the catalase‐immobilized system of CLPSER was compared with divinylbenzene‐crosslinked polystyrene, ethylene glycol dimethacrylate crosslinked polystyrene, and 1,4‐butanediol dimethacrylate crosslinked polystyrene systems. Crosslink levels of 2, 8, and 20 mol % were evaluated. Among these crosslinked systems, the 2 mol % system was found to be most suitable to support catalytic activity. When a long flexible hydrophilic poly(ethylene glycol) crosslink, introduced between the polystyrene (PS) backbone and functional groups was used for immobilization, the extent of coupling and enzyme activity increased. Depending on the nature of the support, the catalytic activity of the system varied. The hydrophilic CLPSER support was most efficient for immobilization compared to the other PS‐based supports. © 2005 Wiley Periodicals, Inc. J Appl Polym Sci 97: 8–19, 2005