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Inhibition of Oxidant-Induced Biochemical Changes of Pork Myofibrillar Protein by Hydrolyzed Potato Protein
- Wang, L.L., Xiong, Y.L.
- Journal of food science 2008 v.73 no.6 pp. C482
- pork, myofibrils, oxidation, oxidants, potato protein, protein isolates, iron, catalysts, thiobarbituric acid-reactive substances, lipid peroxidation, carbonyl compounds, enzyme activity, adenosinetriphosphatase, hydrophobicity, protein hydrolysates, food additives, oxidative stability
- The objective of the study was to investigate the role of hydrolyzed potato protein (HPP) in protecting myofibril protein isolate (MPI) from oxidative modification. MPI prepared from pork muscle was suspended (30 mg protein/mL) in 15 mM piperazine-N, N-bis(2-ethane sulfonic acid) buffer (pH 6.0) with 0, 0.3, 0.75, and 1.5 mg/mL of antioxidative HPP (1-h Alcalase hydrolysate). Oxidation was induced by incubating the protein suspensions at 4 °C for 24 h with (1) an iron-catalyzed oxidizing system (IOS: 0.01 mM FeCl₃, 0.1 mM ascorbic acid, and 1.0 mM H₂O₂) and (2) a metmyoglobin-oxidizing system (MOS: 0.1 mM metmyoglobin and 0.1 mM H₂O₂). Changes in oxidized MPI were measured as thiobarbituric acid-reactive substances (TBARS), protein carbonyl content, Ca- and K-ATPase activities, and ultraviolet (UV) spectra. Oxidation increased the production of TBARS and protein carbonyls by 2.9- and 0.24-fold in IOS and 5.6- and 2.2-fold in MOS, respectively. The 2 oxidizing systems altered the Ca- and K-ATPase activities and exposed hydrophobic groups buried in MPI. The presence of HPP reduced the extent of MPI oxidation in all physicochemical categories tested. Therefore, HPP may be used as a potential functional ingredient in meat products to enhance their oxidative stability.