Antioxidant activity of peptides obtained from porcine myofibrillar proteins by protease treatment.
Hydrolysates obtained from porcine myofibrillar proteins by protease treatment (papain or actinase E) exhibited high antioxidant activity in a linolenic acid peroxidation system induced by Fe(2+). Hydrolysates produced by both papain and actinase E showed higher activities at pH 7.1 than at pH 5.4. The antioxidant activity of the papain hydrolysate was almost the same as that of vitamin E at pH 7.0. These hydrolysates possessed 1,1-diphenyl-2-picrylhydrazyl radical scavenging activity and chelating activity toward metal ions. Antioxidant peptides were separated from the papain hydrolysate by ion exchange chromatography. The acidic fraction obtained by this method exhibited higher activity than the neutral or basic fractions. Antioxidant peptides in the acidic fraction were isolated by high-performance liquid chromatography on an ODS column and shown to possess the structures DSGVT, IEAEGE, DAQEKLE, EELDNALN, and VPSIDDQEELM. The DAQEKLE peptide showed the highest activity among these peptides.
Saiga
Ai
A
Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima, 739-8528, Japan.
Tanabe
Soichi
S
Nishimura
Toshihide
T
D000818:Animals; D000975:Antioxidants / Q000302:isolation & purification / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D010450:Endopeptidases / Q000378:metabolism*; D016166:Free Radical Scavengers; D006863:Hydrogen-Ion Concentration; D009124:Muscle Proteins / Q000737:chemistry* / Q000378:metabolism; D018482:Muscle, Skeletal / Q000378:metabolism*; D009210:Myofibrils / Q000737:chemistry; D010084:Oxidation-Reduction; D010206:Papain / Q000378:metabolism; D011492:Protein Hydrolysates / Q000378:metabolism*; D013552:Swine
D000975:Antioxidants; D016166:Free Radical Scavengers; D009124:Muscle Proteins; D011492:Protein Hydrolysates; D010450:Endopeptidases; D010206:Papain