Solubilisation of myosin in a solution of low ionic strength L-histidine: Significance of the imidazole ring

Xing Chen; Yufeng Zou; Minyi Han; Lihua Pan; Tong Xing; Xinglian Xu; Guanghong Zhou

doi:10.1016/j.foodchem.2015.09.039

Solubilisation of myosin in a solution of low ionic strength L-histidine: Significance of the imidazole ring

Food Chem. 2016 Apr 1:196:42-9. doi: 10.1016/j.foodchem.2015.09.039. Epub 2015 Sep 11.

Authors

Xing Chen¹, Yufeng Zou¹, Minyi Han¹, Lihua Pan¹, Tong Xing¹, Xinglian Xu², Guanghong Zhou¹

Affiliations

¹ Key Laboratory of Animal Products Processing, Ministry of Agriculture, Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Jiangsu Synergetic Innovation Center of Meat Production and Processing, and College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, People's Republic of China.
² Key Laboratory of Animal Products Processing, Ministry of Agriculture, Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Jiangsu Synergetic Innovation Center of Meat Production and Processing, and College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, People's Republic of China. Electronic address: xlxus@njau.edu.cn.

PMID: 26593463
DOI: 10.1016/j.foodchem.2015.09.039

Abstract

Myosin, a major muscle protein, can be solubilised in a low ionic strength solution containing L-histidine (His). To elucidate which chemical constituents in His are responsible for this solubilisation, we investigated the effects of 5mM His, imidazole (Imi), L-α-alanine (Ala), 1-methyl-L-histidine (M-his) and L-carnosine (Car) on particle properties of myosin suspensions and conformational characteristics of soluble myosin at low ionic strength (1 mM KCl, pH 7.5). His, Imi and Car, each containing an imidazole ring, were able to induce a myosin suspension, which had small particle size species and high absolute zeta potential, thus increasing the solubility of myosin. His, Imi and Car affected the tertiary structure and decreased the α-helix content of soluble myosin. Therefore, the imidazole ring of His appeared to be the significant chemical constituent in solubilising myosin at low ionic strength solution, presumably by affecting its secondary structure.

Keywords: 1-Methyl-l-histidine (PubChem CID: 92105); Chemical constituent; Imidazole (PubChem CID: 795); Imidazole ring; Myosin; Solubility; l-Carnosine (PubChem CID: 439224); l-Histidine; l-Histidine (PubChem CID: 6274); l-α-Alanine (PubChem CID: 5950).

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Carnosine
Histidine / analysis
Histidine / chemistry*
Imidazoles / chemistry*
Myosins / chemistry*
Osmolar Concentration
Protein Structure, Secondary
Solubility

Substances

Imidazoles
Histidine
imidazole
Carnosine
Myosins