Inhibitory activity of protein hydrolysates from rice bran on mushroom tyrosinase
- Thaniya Wunnakup, Drug and Herbal Product Research and Development Center, College of Pharmacy, Rangsit University, Patum Thani, Thailand, Corresponding author; E-mail: email@example.com
- Chaowalit Monton, Drug and Herbal Product Research and Development Center, College of Pharmacy, Rangsit University, Patum Thani, Thailand , & Medicinal Cannabis Research Institute, College of Pharmacy, Rangsit University, Patum Thani, Thailand
- Laksana Charoenchai, Drug and Herbal Product Research and Development Center, College of Pharmacy, Rangsit University, Patum Thani, Thailand
Rice bran protein hydrolysates (RBPHs) obtained by Alcalase® have attracted attention because of their bioactivity properties (antioxidant, anti-acetylcholinesterase and anti-butyrylcholinesterase). However, there has been no report on their improved inhibition of melanogenesis. This study aimed to investigate the inhibitory tyrosinase activity of RBPH. The defatted Khao Hom Mali RD15 rice bran protein was extracted into water (RBP1), 2% NaCl (RBP2) and 0.1 N NaOH (RBP3) fractions. All protein fractions were hydrolyzed with Alcalase® to produced RBPH1, RBPH2 and RBPH3. The protein content, % yield, degree of hydrolysis (DH) and molecular weight patterns of each fraction were investigated. The RBPH2 and RBPH3 showed high potential inhibition on mushroom tyrosinase activity, the IC50 values were determined to be 1.92 mg/ml and 0.46 mg/ml, respectively. The inhibition kinetics showed that RBPH2 was an uncompetitive mechanism, with inhibition constants (Ki and Kis) were 6.1 mg/ml and 4.5 mg/ml, respectively. Moreover, the RBPH3 displayed a non-competitive mechanism and Ki and Kis were 2.8 mg/ml and 2.5 mg/ml, respectively. Therefore, the RBPHs could be potential candidates for use in the cosmetics and food industries.
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