Effects of eugenol on the structure and gelling properties of myofibrillar proteins under hydroxyl radical-induced oxidative stress

The effects of eugenol (EG; 0, 5, 20, and 50 mg/g protein) on the structure and gel properties of pork myofibrillar protein (MPs) under a hydroxyl radical-generating system were explored in this study. The results revealed that the addition of a high concentration of EG (50 mg/g protein) markedly reduced the carbonyl content and enhanced the fluorescence intensity, surface hydrophobicity, and protected the secondary structure of MPs, compared to oxidized MPs. In addition, the high concentration group noticeably increased the storage modulus (G '), gel strength, and water-holding capacity (WHC), and significantly hindered the oxidation-induced trans-formation of immobilized water of the MPs gel to free water and basically favored the formation of a finer and more homogeneous three-dimensional network structure, This work verified that the adding of EG could effectively improve the gel quality of oxidized MPs and more successfully delay oxidation-induced damage to muscle protein structure.

Automated summary

This study investigated the effects of eugenol on the structure and gel properties of oxidized pork myofibrillar protein. The results showed that a high concentration of eugenol could protect the protein structure and enhance the gel properties.