Abstract
The hydrolysed collagen has a molecular weight of 3–6 KDa, is soluble in water, colourless and odourless. Hydrolysed collagen was obtained by proteolysis of the native ovine collagen. The enzymatic treatment was carried out with Heliozym under alkaline treatment (pH 8) for different periods of time (0 min, 10 min, 20 min, 30 min, 1 h, 2h, 3h y 4h) at 60°C. The hydroxyproline concentration increased significantly from time 0 min (11.44±2.81 mg/L) to the 4 h (24.47±1.60 mg/L); this change in concentration was observed in the FTIR spectra at a length of 1,037 cm-1 for OH group as well a change in the Amide I (1641 cm-1). The viscosity showed significant differences (P≤ 0.05) between the different hydrolysis times. This parameter was correlated with the molecular weight; when the viscosity was 0 cP the molecular weight showed the lowest value at 5.62 KDa. The antioxidant activity for ABTS radical scavenging showed significant differences (P≤ 0.05) between the times of hydrolysis, the greater the time, the higher the inhibition resulting with 67.61% at the end of the treatment. The DPPH radical scavenging resulted with 27.89 % at the beginning of the hydrolysis. However, the end of the hydrolysis (4h) showed inhibition at 52.75%. The antioxidant activity increased when molecular weight decreased, and this is related with the amino acids present in the peptides obtained for the hydrolysis of the collagen.
