Preparation Of Silver Carp Bone Collagen Peptide And Study On Its Antioxidant Activity
Keywords
Silver Carp Bone, Collagen Peptide, Process Optimization, Isolation And Purification, Antioxidant Activity
Abstract
Abstract Using silver carp bones as raw materials, collagen peptides with high antioxidant activity were prepared through protease enzymatic hydrolysis and Sephadex G-25 gel chromatography separation and purification. First, the yield and hydrolysis degree of collagen peptides were used as evaluation indicators to screen the optimal enzymes from neutral protease, alkaline protease, flavor protease, trypsin and complex protease, and single factor experiments and response surface optimization experiments were used to determine silver carp bone collagen. The best preparation process for polypeptides; Sephadex G-25 gel chromatography was then used for separation and purification to obtain polypeptide components of different molecular weights and analyze their amino acid composition; using ABTS+¡¤scavenging ability and reducing ability as indicators, the silver carp bone collagen polypeptide was investigated Antioxidant activity of each component. The results show that the optimal enzyme for enzymatic hydrolysis of silver carp bone is composite protease, and the optimal process for preparing collagen peptides is as follows: enzyme addition amount is 8 220 U/g, enzymatic hydrolysis temperature is 51¡ãC, and enzymatic hydrolysis time is 4.5 h. The yield of collagen peptide was 49.00%; 5 components were separated by Sephadex G-25, with molecular masses ranging from 14 to 9 788 Da. The amino acid composition is consistent with the characteristics of collagen; antioxidant experiments show that component IV has the strongest ABTS+ ¡¤Scavenging ability and reducing ability, its IC50/OD1.0 are 0.02 mg/mL and 19.16 mg/mL respectively. This study provides technical reference for the development and utilization of fish bone resources
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Original research was done by Zhang Lu, Tu Zongcai, Luo Juan, Li Jun
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