Effect on myofibrillar protein gelation induced by eugenol modification under oxidative stress

Abstract

This study aimed to investigate the effects of eugenol (Eu) at different concentrations (0, 10, 50, 100, 200, and 300 μM/g protein) on the gel properties and chemical structure changes of porcine myofibrillar protein (MP). The results showed that Eu inhibited the increase of surface hydrophobicity and carbonyl content but did not prevent the oxidation-induced loss of thiol groups. Moreover, Eu intensified the loss of the α-helical conformation as well as the tertiary structure of MP under oxidative stress. The physicochemical changes at 10 and 50 μM/g Eu resulted in a significant enhancement of the gelling ability of MP and enhanced the positive role of oxidation in building elastic gel networks. Conversely, Eu at the concentrations of 100, 200, and 300 μM/g was not conducive to gelling ability, especially at 300 μM/g, and these concentrations were associated with Eu-induced protein conformational changes.

Keywords:
eugenol; myofibrillar protein; gelation; rheology properties; conformation