Changes in soy protein immunoglobulin E reactivity, protein degradation, and conformation through fermentation with Lactobacillus plantarum strains
Changes in soy protein immunoglobulin E reactivity, protein degradation, and conformation through fermentation with Lactobacillus plantarum strains
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植物乳杆菌菌株发酵过程中大豆蛋白免疫球蛋白 E 反应性、蛋白质降解和构象的变化
DOI：
10.1016/j.lwt.2018.09.034
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发表时间：
2019-01-01
影响因子：
6
通讯作者：
Dong, Mingsheng
中科院分区：
文献类型：
--
作者：
Rui, Xin;Huang, Jin;Dong, Mingsheng
研究了8株扁平乳杆菌（Lactobacillus planarian）发酵大豆分离蛋白（SPI），降低免疫球蛋白E（IgE）反应性的效果及其与蛋白质降解和构象变化的关系。L.用双抗体夹心酶联免疫吸附试验测定，车前草对IgE反应性的抑制率为83.8%-94.8%。发酵导致可溶性蛋白质含量大幅度降低（53.8%-92.8%），电泳显示几条主要条带，特别是7S α '、α和β亚基的条带强度损失。在某些发酵样品中观察到肽含量增加（< 10 kDa），特别是在L.及MartiniB 1 -6和L. plantarum Y-1。SPI的构象发生了改变，表现为所有发酵样品的表面疏水性改善（1.6-3.3倍）和β链结构的出现。主成分分析证实，肽（< 10 kDa）含量，表面疏水性，和β链与IgE反应性降低密切相关。L. plantarurn可能是由于蛋白质的一级和高级结构的改变。
This study investigated the fermentation of soy protein isolates (SPI) by using 8 Lactobacillus planarian strains, its reduction effect on immunoglobulin E (IgE) reactivity, and its relationship with protein degradation and conformation changes. L. plantarum showed potency in reducing IgE reactivity by 83.8%-94.8%, as determined by sandwich enzyme-linked immunosorbent assay. Fermentation resulted in a great reduction (53.8%-92.8%) in soluble protein content and loss of intensity in several major bands, especially those of 7S alpha', alpha, and beta subunits, as indicated by electrophoresis. Increased peptide (< 10 kDa) content was observed in some fermented samples, especially in those fermented by L. &Martini B1-6 and L. plantarum Y-1. Conformation of SPI was altered, as demonstrated by improved surface hydrophobicity (1.6-3.3 times) and emergence of beta-strand structure in all fermented samples. Principal component analysis confirmed that peptide (< 10 kDa) content, surface hydrophobicity, and beta-strand were closely related to IgE reactivity reduction. The reduction of SPI IgE reactivity by L. plantarurn was probably attributed to the alternation in primary and higher structure of the protein.