Production and purification of antioxidant peptides from flatfish skin protein hydrolysates
Hongji Zhu , Shipeng Wang , Li Tian , Hua Zhang
Transactions of Tianjin University ›› 2015, Vol. 21 ›› Issue (5) : 433 -439.
Antioxidant peptides of flatfish skin protein hydrolyzed by four enzymes(Papain, Pepsin, Trypsin and Neutrase, respectively)were investigated. The Trypsin hydrolysate obtained by hydrolysis exhibited the highest 1,1-dipheny-l-2-picrylhydrazyl(DPPH)radical scavenging activity(DRSA)compared with other hydrolysates. Response surface method ology(RSM), based on Box-Behnken design, was used to study the influence of hydrolysis conditions on the DRSA. The optimal hydrolysis conditions were as follows: pH 7.38, temperature 48.2°C and enzyme/substrate(E/S)ratio 2 840 U/g. Under these conditions, the maximum DRSA was(22.85 ± 0.57)%,. The experimental values agreed with the value (23.09%,)predicted by the model within a 95%, confidence interval. By using gel filtration chromatography and reversed-phase high performance liquid chromatography(RP-HPLC), antioxidant peptide(D2-P)was isolated from flatfish skin protein hydrolysates(FSPH)and could exhibit a(54.28 ± 1.37)%, scavenging activity on DPPH radical at the concentration of 5 mg/mL. This is the first report of a scientific basis for the preparation of antioxidant peptides from flatfish skin. The results suggested that the antioxidant peptides can be exploited into functional foods or used as a novel source of nutraceuticals.
flatfish skin / enzymatic hydrolysis / antioxidant peptides / optimization / purification
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