title: Silk protein, sericin, inhibits lipid peroxidation and tyrosinase activity.
abstract: This study provided the first evidence for an antioxidant action of the silk protein sericin by showing that sericin suppressed in vitro lipid peroxidation. Furthermore, sericin was found to inhibit tyrosinase activity. These results suggest that sericin may be a valuable natural ingredient for food and cosmetic industries.
authors.affiliation: Department of Applied Biochemistry, Faculty of Applied Biological Science, Hiroshima University, Higashi-Hiroshima, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Kato
authors.forename: S
authors.initials: S
authors.lastname: Sato
authors.forename: A
authors.initials: A
authors.lastname: Yamanaka
authors.forename: H
authors.initials: H
authors.lastname: Yamada
authors.forename: N
authors.initials: N
authors.lastname: Fuwa
authors.forename: M
authors.initials: M
authors.lastname: Nomura
mesh_terms: D000818:Animals; D000975:Antioxidants / Q000494:pharmacology*; D012831:Bombyx / Q000737:chemistry; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D019476:Insect Proteins / Q000737:chemistry*; D015227:Lipid Peroxidation / Q000187:drug effects*; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors*; D010456:Peptides, Cyclic / Q000494:pharmacology*; D051381:Rats; D047030:Sericins; D047011:Silk; D017392:Thiobarbituric Acid Reactive Substances / Q000378:metabolism
chemical_list: D000975:Antioxidants; D004791:Enzyme Inhibitors; D019476:Insect Proteins; D010456:Peptides, Cyclic; D047030:Sericins; D047011:Silk; D017392:Thiobarbituric Acid Reactive Substances; D014442:Monophenol Monooxygenase