Extraction and Characterization of Collagen Hydrolysate from Buffalo (Bubalus Bubalis) Skin Including its Antioxidant Properties and Antiarthritic Effect

This study was conducted to characterize the extract collagen hydrolysate (CH) from low value buffalo skin using enzymes bromelain (B) and papain (P), including their bioactivities.

Optimum levels of the two enzymes were determined by Sodium dodecyl sulphate-Polyacrylamide gel electrophoresis (SDS-PAGE) and degree of hydrolysis. Levels (30 and 50 units of B/g of skin and 20 and 30 units of P/g of skin) showing maximum degradation of collagen proteins were used to extract CH and the recovered CH were correspondingly referred as B20, B50, P20 and P30, respectively.

The yield of CH from skin for P20, P30, B30 and B50 was 27.38, 26.32, 20.71 and 16.19%, respectively. SDS-PAGE image of the different CH samples showed complete degradation of α- and β- chains of the collagen protein chains revealing only smear bands. 2, 2-Diphenyl-1-picrylhydrazyl (DPPH) scavenging ability was highest (94.51%) for B50 sample followed by 90.59% for P30 at the concentration of 10 mg/ml. Amide I peaks of various CHs as revealed by fourier-transform infrared spectroscopy (FTIR) showed greater disruption in the triple helical structure of collagen chains in P30 and B50 than P20 and B30 samples. Antiarthritic study revealed that B30 and B50 samples had 71.07 and 99.47% inhibition, respectively at the concentration of 50 µg/ml.

Thus, it could be concluded that 30 and 50 units of papain and bromelain per gram of skin, respectively, could be used to extract CH from buffalo skin and better utilize this high protein byproduct into high value food supplement.