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Title 

Tyrosinase inhibitory polyphenols from roots of Morus ihou

 

뽕나무뿌리로부터 타이로신 저해제인 폴리페놀 화합물의 개발

Authors 

S H JeongYoung Bae RyuM J Curtis-LongH W RyuY S BaekJ E KangWoo Song LeeK H Park

Publisher 

American Chemical Society

Issue Date 

2009

Citation 

Journal of Agricultural and Food Chemistry, vol. 57, no. 4, pp. 1195-1203

Keywords 

flavonoidmorus Ihouphenylbenzofuranslow-bindingtyrosinase

Abstract 

Twelve polyphenols (1-12) possessing tyrosinase inhibitory properties were isolated from the methanol (95%) extract of Morus Ihou. The isolated compounds consisted of four flavanones (1 -4), four flavones (5-8), and four phenylbenzofuranes (9-12). Moracin derivative 12 proved to be new a compound which was fully characterized. Compounds 1-12 were evaluated for both monophenolase and diphenolase (the two steps catalyzed by tyrosinase) inhibition to identify the structural characteristics required for mushroom tyrosinase inhibition. We observed that all parent compounds (1, 5, and 9) possessing an unsubstituted resorcinol group were highly effective inhibitors of monophenolase activity (IC50 values of 1.3, 1.2, and 7.4 μM). The potency of the inhibitors diminished with alkyl substitution on either the aromatic ring or the hydroxyl functions. Interestingly, flavone 5 was shown to possess only monophenolase inhibitory activity, but flavanone 1 and phenylbenzofuran 9 inhibited diphenolase as well as monophenolase significantly. The inhibitory mode of these species was also dependent upon the skeleton: phenylbenzofuran 9 manifested a simple competitive inhibition mode for monophenolase and diphenolase; on the other hand flavanone 1 (monophenolase, K3 = 0.1966 min-1 μM-1 k4= 0.0082 min ∼1, and Kiapp = 0.0468 μM; diphenolase, k3 = 0.0014 min-1 μM-1 k4 = 0.0013 min-1, and Kiapp = 0.8996 μM) and flavone 5 both showed time-dependent inhibition against monophenolase. Compound 1 operated according to the simple reversible slow binding model whereas compound 5 operated under the enzyme isomerization model.

ISSN 

0021-8561

Link 

http://dx.doi.org/10.1021/jf8033286

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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