Article ID Journal Published Year Pages File Type
5132471 Food Chemistry 2018 8 Pages PDF
Abstract

•Raman spectroscopy and SEM were used to observe the changes of G-actin.•Low oxidant concentration accelerated the stretch of G-actin.•High oxidant concentration caused sharp flake aggregation of G-actin.•0-5 mM H2O2 enhanced the binding with alcohols by hydrogen bonds.•1-20 mM H2O2 increased the binding with aldehydes by surface hydrophobicity and aggregation.

To investigate the influence of oxidative modifications of G-actin on its binding ability with aroma compounds, the influence of H2O2 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 0-5 mM H2O2 enhanced the absorption of G-actin toward alcohols involved in the formation of hydrogen bonds by increasing α-helix and carbonyl values. 0-1 mM H2O2 caused the release of aldehydes with decreased sulfhydryl sites. 1-20 mM H2O2 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.

Related Topics
Physical Sciences and Engineering Chemistry Analytical Chemistry
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