Abstract
The oxidative modification of myofibrillar proteins (MPs) has been identified as a crucial factor affecting meat quality during processing. We compared the effects of 4-hydroxy-2-nonenal (HNE) and lipoxygenase (LOX)-catalyzed linoleic acid (LA) oxidation products on the digestibility and gel properties in MPs from bighead carp. Both treatments resulted in decreased free amino acid content, reduced digestibility, and loss of amino acids in MPs. The HNE treatment enhanced gel strength by increasing hydrophobic interactions within the gel matrix. Conversely, the LOX-catalyzed LA oxidation enhanced disulfide bonds, leading to an agglomerated microstructure. Reduced myofibrillar protein (MP) solubility, primarily due to protein aggregation, was observed in the LA group but not in the HNE group. This distinction suggests that the impact on MP functionality is predominantly influenced by the protein aggregation induced by LOX-catalyzed LA oxidation rather than by HNE alone.
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