Glutathione-mediated formation of disulfide bonds modulates the properties of myofibrillar protein gels at different temperatures

Abstract

The present study illustrated modulation of protein aggregation by affecting disulfide/sulfhydryl exchange reactions by adding different concentrations of free thiol represented by reduced-glutathione (GSH) for modulating myofibrillar protein (MP) gel properties at 75 °C or 95 °C. Gel strength and rheological results showed the effects of GSH were dependent on the concentrations (5, 10, 20, 40, and 80 g/kg) and heating temperatures. SEM results showed that the addition of GSH improved the gel microstructure at 95 °C. AFM and DLS results indicated that protein aggregation was also inhibited. At 75 °C, the addition of GSH influenced both MP aggregation and gel properties. Low concentrations (5, 10 g/kg) of GSH promoted aggregation, whereas high concentrations (20, 40, and 80 g/kg) of GSH inhibited this. By analyzing the protein structure and cross-linking pattern changes of MP and MP/GSH composites, a pathway involving GSH influencing MP gel properties was determined.

Keywords: Disulfide bond; Free thiol; Heating temperature; Myofibrillar protein; Protein aggregation; Reaction balance.