Isolation and characterization of collagen from local goat bone using pepsin hydrolysis

Abstract

Goat bone is one of by-product which has not commonly used in Indonesia. Collagen is one of proteins which contained a bone which characterizing its uniq function. The purpose of experiment was to isolate and characterize collagen from local goat bone with pepsin enzymatic hydrolysis in various concentration. The experiment consisted of bone preparation, Isolating by leaching method, and the hydrolysis of collagen bone using pepsin enzyme in various concentration (0.1; 0.3; 0.5; and 1%). Variables observed were collagen yield, soluble protein, pH, Fourier Tansform Infrared Spectroscopy (FTIR) spectra, thermal stability using Differential Scanning Calorimetry (DSC), and molecular weight using Sodium Dodesyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE). The results showed that soluble protein concentration of collagen solution was not affected by pepsin concentrations. The soluble protein of 0.1; 0.3; 0.5 and 1 % of enzym were 0.2030,013; 0.2440,045; 0.2950,065; and 0.2570,066 mg/ml for, respectively. The results of collagen yield was significant, and it were 7.12; 7.54; 13.3; dan 8.81 %. The results of pH showed significant, it was 6.37; 5.96; 6.88; 5.92. The FTIR spectra showed that all of the sample has not changed into gelatin. The thermal stability in DSC analysis showed that the collagen start to gelation at 56.72 to 57.40 C and Tmax for each sample were 128.20; 189.32; 131.35; 124.43 C, respectively. In conclusion, collagen could be isolated from goat bone using enzymatic treatment and showed the fine properties as well as collagen from skin.