溶解度
化学
离子强度
圆二色性
肌原纤维
蛋白质三级结构
离子键合
蛋白质二级结构
赖氨酸
盐桥
生物物理学
结晶学
生物化学
有机化学
水溶液
离子
氨基酸
生物
基因
突变体
作者
Xiuping Li,Wenhui Wang,Shouyin Wang,Yuqing Shen,Jinfeng Pan,Xiuping Dong,Shengjie Li
出处
期刊:Foods
[MDPI AG]
日期:2022-03-17
卷期号:11 (6): 855-855
被引量:7
标识
DOI:10.3390/foods11060855
摘要
This study aimed to investigate the presence of L-lysine (Lys) on the solubility and structures of myofibrillar proteins (MFPs) at different ionic strengths. Porcine MFPs were incubated at 4 °C with various levels of ionic strengths (0.15, 0.3, or 0.6 M NaCl) with or without the presence of 20 or 40 mM Lys. After 24 h of incubation, MFP solubility and turbidity were determined, and the particle size distribution, circular dichroism spectra, and intrinsic tryptophan fluorescence of MFP were analyzed to obtain their secondary and tertiary structure. Results showed that the solubilization effects of Lys on MFPs are dependent on the ionic strength. Particularly, the presence of Lys could improve MFP solubility at 0.3 M, which resembles salt-reducing processing conditions. Concomitantly, the secondary and tertiary structures were observed to change as a result of the varying ionic strengths and the addition of Lys, including myofibril swelling, dissociation of myosin filaments, uncoiling of α-helix, and unfolding of the tertiary structure. The possible mechanisms underlying the solubilization effects of Lys on MFPs at low ionic strengths are discussed from the perspective of protein structural changes.
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