School of Food Science and Engineering, Hefei University o f Technology, Hefei 230009, China.
School of Food Science and Engineering, Hefei University o f Technology, Hefei 230009, China.
Food Chem. 2018 Mar 1;242:22-28. doi: 10.1016/j.foodchem.2017.09.033. Epub 2017 Sep 8.
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.
本文旨在研究 l-赖氨酸(Lys)/l-精氨酸(Arg)对肌球蛋白溶解度的潜在影响机制。结果表明,在考察的 pH 值范围内,Lys 和 Arg 均能提高肌球蛋白的溶解度。此外,Lys 和 Arg 均降低了肌球蛋白的流体力学尺寸,增加了肌球蛋白的水合容量(HC)、表面芳香疏水性、肌球蛋白溶液的表面张力以及构成肌球蛋白的主要氨基酸的绝对转移自由能(TFE)。结果表明,导致肌球蛋白聚集抑制和与疏水氨基酸残基相互作用的 Lys 或 Arg 的特性可能在提高肌球蛋白溶解度方面发挥重要作用。该结果对肉类行业具有吸引力。