Raman spectroscopic study of heat-induced gelation of pork myofibrillar proteins and its relationship with textural characteristic

Abstract

Structural changes, textural properties and their relationships in pork myofibrillar proteins (PMP) were studied by Raman spectroscopy, texture profile analysis (TPA) and principal component analysis (PCA). Raman spectroscopy analysis revealed the occurrence of secondary structural changes in myofibrillar proteins. Modifications in the amide I (1600–1700 cm −1) and amide III (1200–1300 cm −1) regions indicated a significant ( p < 0.05) decrease in α-helix content, accompanied by a significant ( p < 0.05) increase in β-sheets, β-turns and random coil content. Texture property changes were also determined by TPA. All these features contributed to the formation of strong, irreversible heat-induced gels. The application of a dimensionality reducing technique such as PCA proved to be useful to determine the most influential properties of heat-induced gel. Significant ( p < 0.05) correlations were found between these structural changes and the textural characteristic (hardness) in the pork myofibrillar proteins system by PCA.