Bioactivities of Goat Placenta hydrolysates

Abstract

Introduction: Goat placenta is a rich source of proteins and amino acids. It has been reported that low molecular weights of short chain proteins and peptides might possess various bioactivities. Objectives: To investigate some bioactivities of proteins/peptide hydrolysates by papain enzyme. Methods: determination the characteristics of the goat placenta hydrolysates including total protein by Bradford protein assay, molecular weight by Tricine-Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (Tricine-SDS PAGE) and  investigation of antioxidant activities e.g. Free radical scavenging (DPPH),  Inhibition of Linoleic Acid Oxidation and  Ferric Reducing Power as well as anti-mushroom tyrosinase activity. Results: the % yield of the hydrolysates obtained from goat placenta was 18.31±0.42%. The total protein equivalent to bovine serum albumin was 0.075±0.003 mg/ml.  The majority of obtained hydrolysates contained proteins and peptides at a molecular weight of approximately 30 kDa. Antioxidant activities of the hydrolysates were as follows; Free radical scavenging of the hydrolysates at a concentration of 6.25 mg/ml was significantly greater than that of vitamin C at 0.156 mg/ml and was not significantly different from vitamin E acetate at 83.5 mg/ml but less than that of Trolox at 0.156 mg/ml.  Ferric Reducing Power of the hydrolysates at 1.5 mg/ml was equivalent to 15.74 mM Trolox which was less than 0.3 mg/ml of vitamin C. Lipid peroxidation inhibition of the hydrolysates at 1 mg/ml was 84.94% which was not significantly different from that of BHT, Trolox at 0.1 mg/ml and GSH at 1 mg/ml. The hydrolysates at 41.67 mg/ml inhibited 59.11% of mushroom tyrosinase activity. Conclusion: goat placenta proteins/peptide hydrolysates possessed antioxidant activities and anti-tyrosinase activity.