Catalysis of linoleate oxidation by soluble chicken muscle proteins

A soluble fraction of a chickenMusculus gastrocnemius muscle was used to characterize the catalyst of linoleate oxidation. Separation of the chicken muscle extract into low (free metal) and high (protein) molecular weight fractions revealed that the molecular weight of the major catalyst of linoleate oxidation in chicken muscle extract was greater than 700 daltons. Catalysis of linoleate oxidation by the protein fraction exhibited a pH optimum of 5.9. Subjecting the protein fraction to heat treatments at increasing temperatures (30–90 C) decreased the catalysis of linoleate oxidation. Addition of two mM EDTA had no effect on the catalysis of linoleate oxidation. Cyanide (2 mM), glutathione (1 mM) and cysteine (1 mM) decreased the oxidation of linoleate by the protein fraction 21.0%, 22.9% and 29.0% respectively. Characterization of the oxidative catalyst in chicken muscle extract indicated that free metals and hemoproteins contribute to overall catalysis of linoleate oxidation but are not the sole catalysts. Heat inactivation of the oxidative catalyst and the observed pH optimum suggests that the unidentified catalyst is proteinacious and may be an enzyme.