Catalytic activity of aryl alcohol oxidase immobilized in 3D-mesoporous silicates.
Aryl alcohol oxidase was immobilized on two mesoporous materials, MS-A and MS-B. The immobilization rate for the larger pore material MS-A (11.5 nm) was higher than for the smaller pore material MS-B (4.2 nm). Furthermore, the sol-gel silica encapsulation of MS-immobilized enzymes improved thermal stability.
Kato
Katsuya
K
National Institute of Advanced Industrial Science and Technology, Anagahora, Shimoshidami, Moriyama-ku, Nagoya, Japan. katsuya-kato@aist.go.jp
Seelan
Sindhu
S
Saito
Takao
T
D000327:Adsorption; D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010316:Particle Size; D044367:Phase Transition; D017640:Silicates; D013499:Surface Properties
D004800:Enzymes, Immobilized; D017640:Silicates; D000429:Alcohol Oxidoreductases; C077759:aryl-alcohol oxidase