EVALUATION OF BILE ACIDS-BINDING CAPACITY AND TYROSINASE INHIBITOR POTENCY OF NOVEL PEPTIDES PREPARED FROM AGRICULTURAL WASTES VIA ENZYMATIC HYDROLYSIS
REHAB A. AL-AZZOUNY 1, OLA S. ALI 2, SANAA T. EL-SAYED 1*, 1. National Research Centre, Biochemistry Department, 60111, Giza, Egypt
2. Al-Azhar University, Faculty of Pharmacy, Biochemistry Department, 11751, Cairo, Egypt
*Corresponding author: santsayed@yahoo.com
The objective of this study was to prepare bile acids-binding and tyrosinase inhibitory peptides for industrial potential application. Proteins were extracted from Brassica olercea (cauliflower) midribs, Corchorus olitorius (corchorus) stems and Vicia faba (broad bean) leaves then were subjected to hydrolysis by immobilized lettuce protease. For maximum peptides production, the influence of incubation temperatures, and substrate concentrations on the hydrolysis processes were investigated. Peptides were fractionated by ultrafiltration into three fractions according to their molecular weight. Corchorus (fractions F2 and F1) and broad bean (fraction F1) peptides showed bile acids-binding higher than that bind by cholestyramine resin. They may have potential application as a cholesterol-reducing agent for hypercholestermic patients. Cauliflower (F2 and F1) and corchorus (fraction F1) peptides showed tyrosinase inhibitor potency higher than that by kojic acid. They may have potential application as a whitening agent.
