The effect of oxidation on the structure of G-actin and its binding ability with aroma compounds in carp grass skeletal muscle.

To investigate the influence of oxidative modifications of G-actin on its binding ability with aroma compounds, the influence of HO treatments on G-actin structure and the absorption for alcohols and aldehydes was investigated. Raman spectroscopy and scanning electron microscopy were used to evaluate structural changes of G-actin; GC-MS was used to analyze the binding with alcohols and aldehydes. Results showed that 0-5mM HO enhanced the absorption of G-actin toward alcohols involved in the formation of hydrogen bonds by increasing α-helix and carbonyl values. 0-1mM HO caused the release of aldehydes with decreased sulfhydryl sites. 1-20mM HO increased the retention of aldehydes, due to the increased hydrophobic sites by G-actin rebuilding and aggregating. The aggregated G-actin favoured the hydrophobic interactions with aroma compounds, forming the protein-aroma compound complex, thus enhancing the resultant binding ability, as evidenced by scanning electron microscopy and GC/MS analysis.