A collagen was isolated from squid skin, a processing waste product. The biofunctional activities of enzymatic squid skin collagen hydrolysates were determined to produce a value-added material. Five low-molecular-mass hydrolysate fractions, F1 (>30 kD), F2 (10-30 kD), F3 (3-10 kD), F4 (1-3 kD), and F5 (<1 kD), were manufactured from its enzymatic hydrolysate by ultrafiltration. Fraction F3 had the strongest antihyaluronidase inhibitory activity. Gly, Val, and Pro were major amino acids in F3, while Met, Tyr, and His were minor ones. The molecular mass of F3 was in the range of 3.4 to 10 kD. F3 exhibited copper chelating ability in a concentration-dependent manner. The ferrous chelating ability of F3 was almost 50% at 200 µg/mL. F3 also inhibited tyrosinase activity by 39.65% at 1 mg/mL. Furthermore, F3 had stronger hydroxyl radical scavenging activity (IC50 = 149.94 µg/mL) than ascorbic acid (IC50 = 212.94 µg/mL). Therefore, the squid collagen hydrolysate can be utilized as a nutraceutical or cosmeceutical agent.
Keywords: Antioxidant; collagen; hyaluronidase; hydrolysate; squid skin; tyrosinase.