Effects of succinylation on the structure and thermal aggregation of soy protein isolate
Effects of succinylation on the structure and thermal aggregation of soy protein isolate
复制标题
琥珀酰化对大豆分离蛋白结构和热聚集的影响
DOI：
10.1016/j.foodchem.2017.10.137
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发表时间：
2018-04-15
期刊：
影响因子：
8.8
通讯作者：
Guo, Shuntang
中科院分区：
文献类型：
--
作者：
Wan, Yangling;Liu, Jingyuan;Guo, Shuntang
大豆分离蛋白、β -甘氨酸和琥珀酰化水平升高（0-94.88%）的甘氨酸结构控制大豆蛋白热聚集体的形成。此外，在不同温度（70 ~ 100℃）和不同离子强度（0 ~ 1.0 mol/L NaCl）、pH 7.0条件下考察了其热聚集性。结果表明，大豆分离蛋白、β -甘氨酸和甘氨酸在琥珀酰化程度分别达到60%、30%和65%左右时发生了明显的结构变化。之后，酰化率明显下降。在琥珀酰化过程中，大豆蛋白，特别是甘氨酸，其二级和三级结构逐渐受到破坏。因此，甘氨酸的热稳定性降低，而-甘氨酸的热稳定性几乎没有受到影响。然而，由于琥珀酰化大豆分离蛋白的胶体稳定性显著增强，其热聚集明显受到抑制。因此，琥珀酰化可用于提高大豆蛋白在加热后的稳定性。
The structures of soy protein isolate, beta-conglycinin, and glycinin at increasing succinylation levels (0-94.88%) were determined to control the formation of soy protein thermal aggregates. In addition, the thermal aggregation was investigated under various temperatures (70-100 degrees C) and ionic strengths (0-1.0 mol/L NaCl) at pH 7.0. Results showed that soy protein isolate, beta-conglycinin, and glycinin underwent obvious structural changes when their succinylation degrees reached around 60%, 30%, and 65%, respectively. After which, the acylation rates markedly declined. During succinylation, soy proteins, particularly glycinin, endured gradual damages in its secondary and tertiary structures. Consequently, the thermal stability of glycinin was reduced, whereas that of beta-conglycinin was hardly affected. However, as the colloid stability of succinylated soy protein isolate was enhanced significantly, its thermal aggregation was markedly suppressed. Thus, succinylation could be used to improve the stability of soy proteins after heating.