Tyrosinase inhibition by water and ethanol extracts of a Far Eastern sea cucumber, Stichopus japonicus
BACKGROUND: Tyrosinase plays a key role in hyperpigmentaion and enzymatic browning. The present study was aimed at investigating the inhibitory effects of water and 70% aqueous ethanol extracts of Stichopus japonicus, a sea cucumber long consumed as a tonic food and traditional medicine, on the diph...
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Published in | Journal of the science of food and agriculture Vol. 91; no. 9; pp. 1541 - 1547 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Chichester, UK
John Wiley & Sons, Ltd
01.07.2011
Wiley John Wiley and Sons, Limited |
Subjects | |
Online Access | Get full text |
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Summary: | BACKGROUND: Tyrosinase plays a key role in hyperpigmentaion and enzymatic browning. The present study was aimed at investigating the inhibitory effects of water and 70% aqueous ethanol extracts of Stichopus japonicus, a sea cucumber long consumed as a tonic food and traditional medicine, on the diphenolase activity of tyrosinase.
RESULTS: In the tyrosinase inhibition study, high‐performance liquid chromatography completely separated L‐3,4‐dihydroxyphenylalanine and dopachrome from other compounds present in the extracts, and provided more reliable results than the commonly used spectrophotometry. The ethanol extract (IC50 = 0.49–0.61 mg mL−1) showed higher inhibitory activity than the water extract (IC50 = 1.80–1.99 mg mL−1). Enzyme inhibition by the extracts was reversible and of mixed type. For both extracts, the dissociation constants for binding to free enzyme were significantly smaller than those for binding to enzyme–substrate complex. Ethyl‐α‐D‐glucopyranoside (IC50 = 0.19 mg mL−1), isolated for the first time from sea cucumber, and adenosine (IC50 = 0.13 mg mL−1), were identified as key tyrosinase inhibitors.
CONCLUSION: The sea cucumber extracts were demonstrated to possess considerable inhibitory potency against the diphenolase activity of tyrosinase, suggesting that the sea cucumber may be a good source of safe and effective tyrosinase inhibitors. Copyright © 2011 Society of Chemical Industry |
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Bibliography: | ArticleID:JSFA4335 ark:/67375/WNG-NWSVWRNT-H istex:19F1A918B48755BB6843F1950B269090F5D7D126 Regional Technology Innovation Program of the Korean Ministry of Knowledge Economy (MKE) - No. RTI05-01-02 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0022-5142 1097-0010 1097-0010 |
DOI: | 10.1002/jsfa.4335 |