Effect of protein structure on water and fat distribution during meat gelling

Abstract

Emulsion-type sausages were produced, at 80°C for either 0, 10, 20 or 30min, using homogeneous Taihu pork batters. Low-field nuclear magnetic resonance (LF-NMR), with or without deuterium oxide (D2O) substitution, evaluated the proton mobility states related to both water and fat molecules, or fat molecules only, respectively, in the sausage samples, during heat-induced gelation. The decreasing trend in the area proportion of main peak T21, reflected a tighter gel structure in emulsion-type sausages. Raman spectra (400–3600cm–1) revealed decreased α-helix, but increased β-sheet, β-turns and random coil contents, during the gelling process. Moreover, principal component analysis (PCA) showed significant correlations between secondary protein structures with distribution of water and fat in the gel matrix. Furthermore, this study established the relationship of water and fat protons mobility with changes in secondary protein structures, and described the critical time of gel formation in emulsion-type pork sausages.