Heat-induced gel properties of porcine myosin in a sodium chloride solution containing L-lysine and L-histidine. (November 2017)

• Record Type: Journal Article
• Authors: Zhang, Yawei; Wu, Junjun; Jamali, Muneer Ahmed; Guo, Xiuyun; Peng, Zengqi
• Is Part Of: Lebensmittel-Wissenschaft + Technologie =. Volume 85(2017)Part A
• Page Start: 16
• Page End: 21
• Publication Date: 2017-11
• Subjects: Gelled meat products -- Low sodium chloride -- Amino acids -- Gelation behaviour; Food industry and trade -- Periodicals; Food -- Composition -- Periodicals; Microbiology -- Periodicals; Nutrition -- Periodicals; 664.005
• DOI: 10.1016/j.lwt.2017.06.059
• Languages: English
• ISSNs: 0023-6438

Abstract

Abstract: For the development of low sodium gelled meat products, the influence of L-Lys, L-His and L-Lys + L-His on the gelation behaviour and gel properties of porcine myosin in low (1 mmol/L), physiological (0.15 mol/L) and high (0.6 mol/L) NaCl solutions were studied. The dynamic rheological results indicated that the introduction of L-Lys or/and L-His increased the storage moduli change rate (ΔG′) of myosin at 1 mmol/L, 0.15 mol/L and 0.6 mol/L NaCl concentrations. The ΔG' of myosin in the presence of L-Lys was higher than that in the L-His at 1mmol/L- 0.6 mol/L NaCl. A significant increase in gel hardness was observed in the presence of L-Lys or/and L-His (P < 0.05). Compared to the control, L-Lys or/and L-His remarkably reduced the cook loss and improved water-holding capacity of myosin gel at 1 mM NaCl (P < 0.05). Nuclear magnetic resonance (NMR) revealed a distinct increase in the immobile water content with a decrease in the free water in the presence of L-Lys or/and L-His. These findings demonstrated that the introduction of L-Lys or/and L-His have a positive effect on the thermal-induced gelation behaviour and enhanced water binding capacity, contributing to an improvement in the gel properties of myosin, particularly at low NaCl concentrations. Highlights: L-Lys had a greater contribution to rheological behaviour of myosin than L-His. L-His and L-Lys increase ΔG′ and cross-link densities of myosin gel in gelation. The water mobility of myosin gel is weakened in the presence of L-His and L-Lys. L-His and L-Lys improve the gel hardness, WHC and cooking loss of myosin gel. L-His and L-Lys affect the gelation behaviour and promote gel property at 1 mM NaCl.