The study of protein conformation and hydration characteristics of meat batters at various phase transition temperatures combined with Low-field nuclear magnetic resonance and Fourier transform infrared spectroscopy. (15th May 2019)

• Record Type: Journal Article
• Authors: Han, Zongyuan; Zhang, Junlong; Zheng, Jinyue; Li, Xiaojing; Shao, Jun-Hua
• Is Part Of: Food chemistry. Volume 280(2019)
• Page Start: 263
• Page End: 269
• Publication Date: 2019-05-15
• Subjects: Phase transition temperature -- Dynamic rheological property -- Water distribution -- Protein structures -- Low-field nuclear magnetic resonance (Low-field NMR) -- Fourier transform infrared spectroscopy (FT-IR); Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2018.12.071
• Languages: English
• ISSNs: 0308-8146

Abstract

Graphical abstract: Highlights: The transition of sol into gel at phase transition temperatures was demonstrated. At 50 °C, immobilised water was gradually exchanged into free water by Low-field NMR and WHC significantly decreased. By FT-IR, α-helix significantly decreased and α-helix was transformed into β-sheets. The relationship between hydration characteristics and protein conformation was established. Abstract: To get a thorough understanding of evolution of heat-induced gel in meat batters, water distribution, protein conformation and their chemical bonds at phase transition temperatures (20–74 °C) were investigated by Low-field NMR and FT-IR. Firstly, G ′ increased and tan δ decreased beyond 55 °C, when sol was completely changed into an elastic gel. Then water holding capacity (WHC) decreased along with decreasing relaxation time T 22 and a new relaxation time T 23 appeared at 50 °C, which indicated that partially immobilised water was converted into free water outside. Meanwhile, surface hydrophobicity increased significantly and free sulfhydryl contents decreased, which contributed to the formation of disulfide bonds, especially beyond 55 °C. Finally, the transformation of α-helix into β-sheets occurred, and increasing β-sheets are necessary for the formation of elastic gels. Moreover, there was a significant correlation between α-helical contents and water loss, surface hydrophobicity, sulfhydryl contents.