Study on the preparation of collagen peptides from Sardina pilchardus scales and its antioxidant activity
Objective To optimize the preparation of collagen peptides from the scales of Sardina pilchardus and evaluate the antioxidant activities of collagen peptides with different molecular weights.Methods Collagen peptides were extracted from the scales of Sardina pilchardus using enzyme engineering combined with single factor and response surface test,and then separated by ultrafiltration membrane.And the collagen peptides with different molecular weights(10,5,1 kDa)were obtained to analyze the antioxidant activities by free radical chemical system analysis in vitro.Results The yield rate of collagen peptides was highest when hydrolyzed by alkaline protease.The optimal enzymatic hydrolysis conditions were determined as follows:The dosage of alkaline protease was 7526 U/g,solid-liquid ratio of 1:20(g/mL),pH 10.5,hydrolysis temperature of 67℃,and hydrolysis time of 4 h.Under these conditions,the yield of collagen peptides from fish scales reached a maximum of 43.44%±1.59%.The scavenging capacity of collagen peptides with a molecular weight of less than 1 kDa against 1,1-diphenyl-2-trinitrophenyl hydrazine radical 1,1-diphenyl-2-picrylhydrazyl(DPPH)radical and hydroxyl radicals hydroxyl radical(·OH)were strongest,with the half maximal inhibitory concentration(IC50)of 0.72 and 1.76 mg/mL,respectively;the scavenging capacity of collagen peptides with a molecular weight of 1-5 kDa against superoxide anion radicals superoxide radical(O2-·)was highest,with the IC50 of 1.45 mg/mL.Conclusion Alkaline protease can effectively prepare fish scale collagen peptides,and fish scale collagen peptides with less than 1 kDa have the best antioxidant activity.
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