Modification of myofibrillar protein gelation under oxidative stress using combined inulin and glutathione

The effects of inulin (1.5%), glutathione (GSH, 0.05%), and their combination (1.5% inulin + 0.05% GSH) on the conformational structure and gel performance of pork myofibrillar protein (MP) under oxidation condition were examined. The addition of GSH significantly prevented oxidation-induced carbonylation, reduction of alpha-helix content, and protein aggregation. As a result, treatment with GSH significantly reduced the particle size of oxidized MP by 35%, increased the solubility by 17.3%, and improved the gelling properties. The presence of inulin also obviously enhanced the gelling behavior of MP under oxidation condition, although it could hardly inhibit the modification of MP structure caused by oxidation. Treatment with inulin + GSH exhibited the highest cooking yield (84.2%) and the best textural characteristics, with a denser and more uniform network structure comprising evenly distributed small pores. The findings of this study provide a useful method for processing meat protein gel products with better oxidative stability and textural properties.

Automated summary

The effects of inulin, glutathione, and their combination on the structure and gel properties of oxidized pork myofibrillar protein were investigated. Glutathione prevented protein oxidation and aggregation, while inulin enhanced the gel behavior of the protein. Treatment with inulin and glutathione together resulted in the highest cooking yield and improved texture characteristics.