Extraction, Purification and Characterization of Collagen Peptide Prepared from Skin Hydrolysate of Sturgeon Fish

Abstract Collagen peptides from marine organisms have drawn great attention in food, cosmetics and medicine owing to their multiple functions including antioxidant, anticancer, cardioprotection, skin protection, wound healing effects. Recent reports revealed that a large amount of solid waste is discarded fisheries could be used for producing high value-added products. This study aims extract purify collagens sturgeon fish skin, by-product obtained during the processing fish. A yield acid-soluble collagen was by using acetic acid extraction followed sonication, while pepsin-soluble (PSC) shown sonication adding pepsin residue then sonication. Two-stage hydrolysis with first flavourzyme necessary produce PSC peptide. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis presence type I structural integrity confirmed Fourier transform infrared spectroscopy analysis. Flavourzyme more effective hydrolyzing into low molecular weight (MW) than pepsin, papain, alcalase, trypsin. Purification hydrolysate Sephadex G-10 column exclude peptide MW>700 Da or ultrafiltration dialysis membrane MW cutoff 500 produced MW<700 MW<728 accounting, respectively, accounting 40% 52% all fragments based on resolution-matrix assisted laser desorption/ionization-mass spectrometry (LR-MALDI-MS). In conclusion, as raw material level 5%, highest degree controlling pH at 8, temperature 50 °C, ratio deionized water 1:40 (mass concentration), time 4 h, dialyzing Da.