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

被引：115
作者：
Chen, Xing
Zou, Yufeng
Han, Minyi
Pan, Lihua
Xing, Tong
Xu, Xinglian [1 ]
Zhou, Guanghong
机构：
[1] Nanjing Agr Univ, Jiangsu Synerget Innovat Ctr Meat Prod & Proc, Key Lab Meat Proc & Qual Control, Key Lab Anim Prod Proc,Minist Agr,Minist Educ, Nanjing 210095, Jiangsu, Peoples R China
来源：
FOOD CHEMISTRY | 2016年 / 196卷
基金：
中国国家自然科学基金;
关键词：
Myosin; L-Histidine; Imidazole ring; Solubility; Chemical constituent; PORCINE MYOSIN; SALT-SOLUTION; PH; PROTEIN; ROD; SUBFRAGMENTS; AGGREGATION; FILAMENTS; PRESSURE;
D O I：
10.1016/j.foodchem.2015.09.039
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
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 5 mM His, imidazole (Imi), L-alpha-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 KCI, 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 a-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. (C) 2015 Elsevier Ltd. All rights reserved.
引用
收藏
页码：42 / 49
页数：8
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