Premium
Stability and activity of chymotrypsin immobilized on magnetic nanogels covered with carboxyl groups
Author(s) -
Hong Jun,
Huang Jin,
Liu Shunying,
Yu Jiahui,
Luo Shufang
Publication year - 2008
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.29325
Subject(s) - immobilized enzyme , chymotrypsin , substrate (aquarium) , chemistry , enzyme , polymer chemistry , hydrolysis , casein , enzyme assay , polymerization , denaturation (fissile materials) , organic chemistry , nuclear chemistry , trypsin , polymer , oceanography , geology
α‐chymotrypsin as model enzyme was anchored to the carboxyl‐functionalized magnetic nanogels prepared by in situ photochemical polymerization. Furthermore, to explore the optimum immobilization, the effects of immobilization time, pH of the reaction mixture, and proportion of enzyme to the magnetic nanogels were studied. The immobilized enzyme was stable in the presence of enzyme denaturation surfactants, and maintained their activity against protein‐digesting enzyme. The immobilized enzyme exhibited hydrolysis activity against the substrate of casein, and cleaved the substrate into small fragments. © 2008 Wiley Periodicals, Inc. J Appl Polym Sci, 2009