PubAg

Main content area

l- Lysine and l-arginine inhibit myosin aggregation and interact with acidic amino acid residues of myosin: The role in increasing myosin solubility

Author:
Li, Shiyi, Zheng, Yadong, Xu, Peng, Zhu, Xiaoxu, Zhou, Cunliu
Source:
Food chemistry 2018 v.242 pp. 22-28
ISSN:
0308-8146
Subject:
Gibbs free energy, arginine, hydrodynamics, hydrophobicity, livestock and meat industry, lysine, myosin, pH, solubility, surface tension
Abstract:
The objective of this paper is to investigate the potential affecting mechanisms of l-lysine (Lys)/l-arginine (Arg) on myosin solubility. The results showed that both Lys and Arg increased the solubility of myosin at the examined pH values. Additionally, both Lys and Arg decreased the hydrodynamic size of myosin but increased the hydration capacity (HC), the surface aromatic hydrophobicity of myosin, the surface tension of the myosin solution and the absolute transfer free energy (TFE) of the major amino acids that constitute myosin. The results indicate that the properties of Lys or Arg that result in an inhibition of myosin aggregation and an interaction with hydrophobic amino acid residues may play important roles in increasing the myosin solubility. The results are attractive to the meat industry.