Mechanism of structural interplay between rice proteins and soy protein isolates to design novel protein hydrocolloids

Mechanism of structural interplay between rice proteins and soy protein isolates to design novel protein hydrocolloids
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大米蛋白和大豆分离蛋白之间的结构相互作用机制设计新型蛋白质亲水胶体

DOI:
10.1016/j.foodhyd.2018.06.024
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发表时间:
2018-11
期刊:
影响因子:
10.7
通讯作者:
Ren Wnag
Ren Wnag
中科院分区:
农林科学1区
文献类型:
--
作者:
Tao Wang;Pengcheng Xu;Zhengxing Chen;Ren Wnag

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食品蛋白质的水溶性对其起泡和乳化等功能起着重要作用,特别是对于那些具有高表面疏水性的蛋白质。将大米蛋白(RPs)和大豆分离蛋白(SPI)按质量比1:0.1(R/S)在pH 12下共溶1h,室温下调至pH 7,RPs的水溶性由1.84%提高到82%以上。荧光光谱和近紫外圆二色性谱表明,在碱变性条件下,RP和SPI的未折叠主链通过氢键相互作用,折叠在一起掩埋非极性基团,而暴露极性基团。由于结构强度显着提高,交联结构失去了对随后酸复化的敏感性,并通过蛋白质体内的疏水和离子相互作用被包装成尺寸在80至130 nm之间的轮廓分明的颗粒。在球形外壳周围形成具有相当大的表面电荷的螺旋片段,保护了结构免受合并和聚集。该方法的简单性和有效性表明,它是食品工业和其他相关领域高通量修饰不溶性可食用蛋白质为水胶体的极好策略。
Water solubility of food proteins plays a significant role in their functionalities like foaming and emulsifying, especially for those with high surface hydrophobicity. In this paper, we report that by co-dissolving rice proteins (RPs) and soy protein isolates (SPIs) upon a mass ratio of 1:0.1 (R/S) at pH 12 for 1 h, followed by readjusting to pH 7 at ambient temperature, the water solubility of RPs was enhanced to be over 82% (from 1.84%). Fluorescence and near-UV CD spectra demonstrated that, under alkali denaturation, the unfolded backbones of RPs and SPIs interacted via hydrogen bonding, and folded together to bury apolar groups whereas expose polar moieties. The cross-linked structures lost the susceptibility to the subsequent acid renaturation due to significantly improved structural strength, and were packed into well-defined particles sized between 80 and 130 nm by hydrophobic and ionic interactions inside the protein bodies. The formation of helix segments with considerable surface charges around the spherical exteriors protected the architectures against merging and aggregation. The simplicity and effectiveness of this protocol suggest that it is an excellent strategy for the high-throughput modification of insoluble edible proteins toward hydrocolloids in food industry and other relevant areas.
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