Enzymatic synthesis of a catechin conjugate of polyhedral oligomeric silsesquioxane and evaluation of its antioxidant activity.
The antioxidant activity of catechin was amplified by conjugation with amine-terminated polyhedral oligomeric silsesquioxane (POSS) using horseradish peroxidase as catalyst. Compared to intact catechin, the scavenging activity of the POSS-catechin conjugate against superoxide anion was greatly improved. In addition, the conjugate strongly inhibited xanthine oxidase activity.
Ihara
N
N
Department of Materials Chemistry, Graduate School of Engineering, Kyoto University, Kyoto, 615-8510, Japan.
Kurisawa
M
M
Chung
J E
JE
Uyama
H
H
Kobayashi
S
S
D000975:Antioxidants / Q000737:chemistry* / Q000494:pharmacology*; D002384:Catalysis; D002392:Catechin / Q000031:analogs & derivatives* / Q000096:biosynthesis / Q000737:chemistry / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology; D016166:Free Radical Scavengers / Q000737:chemistry / Q000494:pharmacology; D006735:Horseradish Peroxidase; D015394:Molecular Structure; D017646:Organosilicon Compounds / Q000737:chemistry* / Q000494:pharmacology*; D013481:Superoxides; D014969:Xanthine Oxidase / Q000037:antagonists & inhibitors
D000975:Antioxidants; D004791:Enzyme Inhibitors; D016166:Free Radical Scavengers; D017646:Organosilicon Compounds; D013481:Superoxides; D002392:Catechin; D006735:Horseradish Peroxidase; D014969:Xanthine Oxidase