Proteomic study of the effect of different cooking methods on protein oxidation in fish fillets

Abstract

The effect of different cooking methods on protein and lipid oxidation of farmed sturgeon (Acipenser gueldenstaedtii) was investigated. In this study, the fish fillets were cooked using five different methods (boiling, steaming, microwaving, roasting and deep-frying), to an internal temperature of approximately 85 °C. General indexes for protein oxidation (carbonyls, free thiols and Schiff bases) and lipid oxidation were evaluated by spectrophotometric and fluorimetric methods. Side-chain modifications of amino acid residues were pinpointed by gel- and MS-based proteomic technology. The results are as follows: (1) cooking, especially roasting and frying, significantly increased the levels of carbonyls and Schiff bases and decreased the amounts of free thiols. (2) Oxidation of aromatic amino acids and extensive oxidation of lysine to carbonyl-containing compounds were characterized in all the cooked samples. (3) Indirect protein oxidation caused by interacting with lipid-derived aldehydes like malondialdehyde (MDA) and 4-hydroxynonenal (HNE) was also observed and much more pronounced in roasted and fried samples, giving a footprint of lipid–protein interaction during cooking. In summary, cooking treatment can induce protein oxidation in sturgeon fillets with a variety of modifications occurring at the protein primary structure. Molecular mapping of protein oxidation is conducive to understand the mechanism of cooking-induced protein oxidation and allows better control of the nutritional properties of protein-based products.