Premium
Immobilization of α‐chymotrypsin onto hydrolyzed poly(ethylene)‐ g ‐co‐hydroxyethyl methacrylate
Author(s) -
Da Silva M. Alves,
Gil M. H.,
Guiomar A. J.,
Martins C.,
Guthrie J. T.
Publication year - 1990
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.1990.070410722
Subject(s) - carbodiimide , chymotrypsin , copolymer , hydrolysis , polymer chemistry , immobilized enzyme , methacrylate , 2 hydroxyethyl methacrylate , ethylene , chemistry , nuclear chemistry , materials science , enzyme , polymer , catalysis , organic chemistry , trypsin
α‐Chymotrypsin has been immobilized onto partially hydrolyzed poly(ethylene)‐ g ‐co‐hydroxyethyl methacrylate (120% graft), using 1‐cyclohexyl‐3‐(2‐morpholinoethyl)‐carbodiimide‐ p ‐toluene‐sulphonate (CMC) as the activating agent. The influence of the enzyme concentration, the carbodiimide concentration, and the coupling medium on the immobilization reaction was studied. A system with 160 mg of coupled enzyme per gram copolymer, providing 126 mg of active enzyme per gram of copolymer was obtained. The K M , V max , and the optimum temperature profile and optimum pH value for the free and immobilized α‐chymotrypsin were determined.