Heteroprotein complex of soy protein isolate and lysozyme: Formation mechanism and thermodynamic characterization

化学 等温滴定量热法 溶菌酶 静电 静电学 氢键 大豆蛋白 微尺度化学 疏水效应 熵(时间箭头) 滴定法 静电相互作用 结晶学 色谱法 物理化学 分子 有机化学 热力学 化学物理 生物化学 数学教育 工程类 物理 电气工程 数学
作者
Jiabao Zheng,Chuan‐He Tang,Ge Ge,Mouming Zhao,Weizheng Sun
出处
期刊:Food Hydrocolloids [Elsevier BV]
卷期号:101: 105571-105571 被引量:30
标识
DOI:10.1016/j.foodhyd.2019.105571
摘要

The electrostatic assembly between heteroproteins is one of the most important applications of associative interaction. The present study investigated the effects of pH and NaCl on the formation rules, phase behavior, and thermodynamic changes of soy protein isolate (SPI)/lysozyme (LYS) complexes. The hydrodynamic diameter of SPI significantly increased as pH was lowered to 6.5, whereas that of LYS significantly increased at pH ≥ 7.5, as a result of self-aggregation. Electrostatic assembly between SPI and LYS completely complies with the charge compensation, producing nanoscale (about 200 nm) and microscale (about 5 μm) complexes at different mixing ratio. However, NaCl can lower ζ-potential of SPI and LYS, and weaken the electrostatic interaction between heteroproteins. The presence of 200 mM NaCl can completely inhibit the electrostatic assembly between SPI and LYS (1 mg/mL). Not only electrostatic interactions but also hydrogen bonds participated in the complex. As the observation of phase-contrast mode, the pH, stoichiometry, NaCl, and assembling time significantly affected size and shape of SPI/LYS complexes, whereas all SPI/LYS complexes exhibited solid-liquid phase separation on the time scale of 0–60 min. Isothermal titration calorimetry analysis indicated that SPI/LYS complex was thermodynamically favored (ΔG < 0), both the exotherm (ΔH < 0) and the entropy gain contributed to SPI/LYS assembling while the entropy gain might be the dominant term. Moreover, the absolute values of ΔG, ΔH, and ΔS significantly decreased with increasing NaCl concentration.
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