Abstract During the processing of jumbo squid (Dosidicus gigas), a large number of byproducts are generated, one of which is a source of collagen. Through controlled hydrolysis, collagen can be used to obtain peptides with antioxidant activity. However, the magnitude of its hydrolysis depends on the degree of cross-linking of its collagen fibres. Connective tissue proteins were extracted, fractionated, and separated according to their solubility and degree of cross-linking (borate-soluble collagen (BSC) low or not cross-linked, acid-soluble collagen moderately cross-linked, and insoluble collagen highly cross-linked), followed by sequential hydrolysis using pepsin, trypsin, and chymotrypsin. The hydrolysis of BSC in connective tissue was greater. BSAC was found to have a higher percentage of antioxidant activity in the ABTS·+ (2,2-azino-bis-3-ethylbenzothiazoline-6-sulphonic acid), with maxima of 92%. Moreover, the evaluation of antioxidant activity suggested that the lower the degree of collagen cross-linking was, the greater the degree of protein hydrolysis.
Villalba-Urquidy et al. (Mon,) studied this question.