Heteroprotein complex formation of soy protein isolate and lactoferrin: Thermodynamic formation mechanism and morphologic structure
Heteroprotein complex formation of soy protein isolate and lactoferrin: Thermodynamic formation mechanism and morphologic structure
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大豆分离蛋白和乳铁蛋白异质蛋白复合物的形成：热力学形成机制和形态结构
DOI：
10.1016/j.foodhyd.2019.105415
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发表时间：
2020-03
影响因子：
10.7
通讯作者：
Sun Weizheng
中科院分区：
文献类型：
--
作者：
Zheng Jiabao;Gao Qing;Tang Chuan-he;Ge Ge;Zhao Mouming;Sun Weizheng
异蛋白复合凝聚层（HPCC）是一种最有前途的静电驱动生物高分子材料。研究了大豆分离蛋白/乳铁蛋白复合凝聚层的形成条件、热力学形成机理及形态结构。在最佳条件下制备的SPI/LF复合凝聚层呈电中性，且遵循电荷补偿原理。电泳和等温滴定量热法验证了所有的SPI组分都参与了HPCC，并且SPI/LF复合物的化学计量与它们的最佳混合比相同。此外，SPI/LF复合凝聚过程中的熵增益（TΔS > 0）和负焓变（ΔH < 0）对复合凝聚过程有利（ΔG <0）。复合凝聚过程中不仅存在静电作用，而且存在氢键作用。SPI/LF的相互作用提高了LF热敏叶的热稳定性。此外，SPI/LF复合物（pH 6.25，SPI/LF = 1：3）呈现出明显的颗粒，而SPI/LF复合物（pH 6.6，SPI/LF = 1：4）呈现出均匀的交联结构。原子力显微镜观察表明，在pH6.25-SPI/LF = 1：3条件下，形成了直径为50-150 nm的球形复合物;在pH6.6-SPI/LF = 1：4条件下，形成了长50-150 nm、宽20-80 nm的链状复合物。
Heteroprotein complex coacervate (HPCC) is one of the most promising electrostatically driven biopolymer materials. In this paper, the formation conditions, thermodynamic formation mechanism, and morphologic structure of soy protein isolate/lactoferrin (SPI/LF) complex coacervate were investigated. The SPI/LF complex coacervates prepared under optimal conditions were electrically neutral and followed the principle of charge compensation. Electrophoresis and isothermal titration calorimetry verified that all individual SPI fractions participated in HPCC and the stoichiometry of the SPI/LF complexes was the same as their optimal mixing ratio. Moreover, SPI/LF complex coacervation was thermodynamically favoured (ΔG < 0), which resulted from entropy gain (TΔS > 0) and negative enthalpy change (ΔH < 0). Not only electrostatic interactions but also hydrogen bonds participated in the complex coacervation. The SPI/LF interaction improved the heat-stability of heat-sensitive lobe in LF. Furthermore, the SPI/LF complex (pH 6.25, SPI/LF = 1:3) exhibited distinct granules, whereas the uniform crosslinking structure appeared in the other SPI/LF complex (pH 6.6, SPI/LF = 1:4). Atomic force microscope showed the sphere complex (pH 6.25-SPI/LF = 1:3) with a diameter of 50–150 nm and the chain-like complex (pH 6.6-SPI/LF = 1:4) with a length of 50–150 nm and a width of 20–80 nm.
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影响因子：
15
作者：
Fu, Jingcheng;Schlenoff, Joseph B.
通讯作者：
Schlenoff, Joseph B.
影响因子：
5.6
作者：
Moore, SA;Anderson, BF;Baker, EN
通讯作者：
Baker, EN
影响因子：
10.7
作者：
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通讯作者：
Monique Barreto Santos;C. W. P. D. Carvalho;E. Garcia-Rojas
影响因子：
6.1
作者：
Guangyan Qi;K. Venkateshan;Xiaoqun Mo;Lu Zhang;X. Sun
通讯作者：
Guangyan Qi;K. Venkateshan;Xiaoqun Mo;Lu Zhang;X. Sun
DOI：
10.1016/j.ijbiomac.2006.06.013
发表时间：
2007-01
影响因子：
8.2
作者：
Chuan-he Tang;Siu-Mei Choi;C. Ma
通讯作者：
Chuan-he Tang;Siu-Mei Choi;C. Ma