Characteristics of immobilized aminoacylase from Aspergillus oryzae on macroporous copolymers.
Aminoacylase from Aspergillus oryzae was adsorbed on functionallized macroporous copolymers where the enzyme showed excellent catalyzing activity and operation stability. Various factors which effect the activity of the immobilized aminoacylase such as temperature, pH and ionic strength were investigated. The continuous operation of the enzyme immobilized on macroporous copolymers was compared with that of the enzyme immobilized on DEAE-Sephadex.
He
B L
BL
Institute of Polymer Chemistry, Nankai University, Tianjin, China.
Jiang
P
P
Qiu
Y B
YB
D000581:Amidohydrolases / Q000378:metabolism*; D001236:Aspergillus oryzae / Q000201:enzymology; D003637:DEAE-Dextran; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007477:Ions; D011108:Polymers; D013696:Temperature
D004800:Enzymes, Immobilized; D007477:Ions; D011108:Polymers; D003637:DEAE-Dextran; D000581:Amidohydrolases; C019672:aminoacylase I