FOOD SCIENCE ›› 2026, Vol. 47 ›› Issue (8): 19-31.doi: 10.7506/spkx1002-6630-20251112-097

• Food Colloids: Component Interaction, Structural Design and Nutrition • Previous Articles    

Effects of Low-Sodium Salt Mixture Combined with L-Lysine or L-Arginine on the Structure and Gel Properties of Myofibrillar Protein

WU Yannan, WU Yue, WANG Wei, LI Ming, LIU Miaomiao, JU Yunlong, LI Yuanzheng, CAO Yungang   

  1. (1. School of Food Science and Engineering, Shaanxi University of Science & Technology, Xi’an 710021, China; 2. Linyi Jinluo Win Ray Food Co., Ltd., Linyi 276000, China)
  • Published:2026-05-15

Abstract: This study investigated the effects of a low-sodium salt mixture (0.4 mmol/L, concentration ratio of NaCl to KCl = 2:1) added with L-lysine (L-Lys) or L-arginine (L-Arg) at concentrations of 1, 3, and 5 mmol/L on the structure and gel properties of myofibrillar protein (MP) using the salt mixture added with 1 mmol/L pyrophosphate (PP) as the control. The results indicated that compared with conventional salt treatment (0.4 mol/L NaCl + 1 mmol/L PP), the low-sodium salt + PP treatment slightly but not significantly improved the water-holding capacity, texture, and rheology of MP gels. Compared with its combination with PP, the low-sodium salt mixture combined with basic amino acids (L-Lys and L-Arg) promoted the transformation of α-helix into other secondary structures and induced alterations in the surface properties of MP. Furthermore, the addition of L-Arg significantly reduced the average particle size and increased the solubility of MP. The addition of 5 mmol/L L-Arg decreased the average particle size by 22.1% and elevated the solubility by 330.9% (P < 0.05). The incorporation of basic amino acids enhanced the storage modulus (G’), reduced the cooking loss, and improved the water-holding capacity of MP gels. Low-field nuclear magnetic resonance (LF-NMR) analysis revealed that the addition of basic amino acids resulted in an overall shortening of the relaxation time of immobilized water in MP gels, which signifies a reduction in the mobility of water molecules within the gel matrix. Scanning electron microscopy (SEM) showed that the addition of basic amino acids promoted the formation of a more fine, uniform and compact microstructure during the heat-induced gelation of MP. In conclusion, basic amino acids (especially L-Arg) can significantly improve the solubility and gel properties of MP under the condition of “low sodium and no phosphorus”, which provides a theoretical basis and reference for the development of healthy meat products.

Key words: myofibrillar protein; L-lysine; L-arginine; gel performance; rheological properties

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