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    Item type:Publication,
    Production of collagen hydrolysate with antioxidant activity from pharaoh cuttlefish skin
    (2016-05-01)
    Bousopha, Sophawan
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    The aim of this study was to produce collagen hydrolysate with antioxidant activity. Pepsin soluble collagen (PSC) isolated from the skin of Pharaoh cuttlefish (Sepia pharaonis) was used as a substrate for hydrolysis at 25°C and pH 7.5 by using collagenase from Clostridium histolyticum. The result showed that rapid hydrolysis was observed within the first 90 min with a degree of hydrolysis (DH) approaching 35%. Thereafter, a slower rate of hydrolysis was generally observed. An increase in DH was generally observed with increasing enzyme concentration. When log10 (collagenase concentration) versus DH (%) was plotted, a linear relationship was found with a coefficient of determination (R2) of 0.9863. Electrophoretic study of collagen hydrolysates with 10% DH, 20% DH, and 30% DH revealed that their major peptides had molecular weights (Mr) ranging from 6.5 to 10.3 kDa; and 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and 2,2-diphenyl-1-picryl hydrazyl (DPPH) radical scavenging activities. The ferric reducing activity power (FRAP) of collagen hydrolysates with 20% DH and 30% DH were similar (p > 0.05). Chelating activity of collagen hydrolysates with 20% DH was negligible and for 10% DH and 30% DH it was not detectable. Given these findings, Pharaoh cuttlefish skin, a byproduct of cuttlefish processing, is a promising source material for production of collagen hydrolysate with antioxidant activities.