Study on immobilization of aminoacylase from Aspergillus oryzae on macroporous copolymers.
The aminoacylase from Aspergillus oryzae was adsorbed on polymer carriers where the enzyme showed excellent catalyzing activity and operating stability. It was found that the pore structure and functional group were the basic factors which affected the activity of the adsorbed enzyme. The hydrophobility of the carriers did not play an important role in the enzymatic resolution. Various factors, such as percentage and nature of cross-linking agent, porogenic agents and functionalizing agents which controlled the pore structure and properties of the polymer carriers during their preparation, were investigated and relationship between the activity of the adsorbed aminoacylase and the carrier structure was also discussed.
He
B L
BL
Institute of Polymer Chemistry, Nankai University, Tianjin, P.R. China.
Jiang
P
P
Qiu
Y B
YB
D000327:Adsorption; D000581:Amidohydrolases; D001230:Aspergillus / Q000201:enzymology*; D001236:Aspergillus oryzae / Q000201:enzymology*; D004800:Enzymes, Immobilized; D011108:Polymers; D011137:Polystyrenes
D004800:Enzymes, Immobilized; D011108:Polymers; D011137:Polystyrenes; D000581:Amidohydrolases; C019672:aminoacylase I