TitleIsolation and Identification of Tyrosinase-Inhibitory and Copper-Chelating Peptides from Hydrolyzed Rice-Bran-Derived Albumin.
Publication TypeJournal Article
Year of Publication2018
AuthorsKubglomsong S, Theerakulkait C, Reed RL, Yang L, Maier CS, Stevens JF
JournalJ Agric Food Chem
Date Published2018 Aug 08
KeywordsAlbumins, Amino Acid Sequence, Chelating Agents, Copper, Enzyme Inhibitors, Hydrolysis, Monophenol Monooxygenase, Oryza, Peptides, Plant Proteins, Seeds

Rice-bran albumin (RBAlb), which shows higher tyrosinase-inhibitory activity than other protein fractions, was hydrolyzed with papain to improve the bioactivity. The obtained RBAlb hydrolysate (RBAlbH) was separated into 11 peptide fractions by RP-HPLC. Tyrosinase inhibition and copper chelation activities decreased with increasing retention times of the peptide fractions. RBAlbH fraction 1, which exhibited the greatest activity, contained 13 peptides whose sequences were determined by using LC-MS/MS. Most of the peptide sequences contained features of previously reported tyrosinase-inhibitory and metal-chelating peptides, especially peptide SSEYYGGEGSSSEQGYYGEG. RBAlbH fraction 1 showed more effective tyrosinase inhibition (IC = 1.31 mg/mL) than citric acid (IC = 9.38 mg/mL), but it was less effective than ascorbic acid (IC = 0.03 mg/mL, P ≤ 0.05). It showed copper-chelating activity (IC = 0.62 mg/mL) stronger than that of EDTA (IC = 1.06 mg/mL, P ≤ 0.05). These results suggest that RBAlbH has potential as a natural tyrosinase inhibitor and copper chelator for application in the food and cosmetic industries.

Alternate JournalJ. Agric. Food Chem.
PubMed ID30016586
PubMed Central IDPMC6431294
Grant ListS10 OD020111 / OD / NIH HHS / United States