Structural rearrangement of ethanol-denatured soy proteins by high hydrostatic pressure treatment.
Structural rearrangement of ethanol-denatured soy proteins by high hydrostatic pressure treatment.
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DOI：
10.1021/jf201957r
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发表时间：
2011-06
影响因子：
6.1
通讯作者：
Jinmei Wang;Xiaoquan Yang;S. Yin;Yehui Zhang;Chuan-he Tang;Bian-Sheng Li;De-Bao Yuan;Jian Guo
中科院分区：
文献类型：
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作者：
Jinmei Wang;Xiaoquan Yang;S. Yin;Yehui Zhang;Chuan-he Tang;Bian-Sheng Li;De-Bao Yuan;Jian Guo
采用差示扫描量热法、傅里叶变换红外光谱和紫外光谱研究了高静水压力（100-500 MPa）处理对乙醇（EtOH）变性大豆β-甘氨酸和甘氨酸的溶解度和结构性质的影响。在200 MPa以上，特别是在中性、碱性和低离子强度条件下，HHP处理显著提高了变性大豆蛋白的溶解度。变性β-甘氨酸在高压作用下发生结构重排，焓值升高（ΔH），形成有序的超分子结构，分子内氢键更强。高压处理（200-400 MPa）导致β-甘氨酸的表面疏水性（F(max)）增加，部分原因是暴露于Tyr和Phe残基，而高压处理（500 MPa）由于疏水重排导致F（max）降低。β-甘氨酸中的色氨酸残基逐渐转移到疏水环境中，这可能进一步支持结构重排的发现。相反，不断增加的压力诱导变性甘氨酸的逐渐展开，并伴随着Tyr和Phe残基向蛋白质分子表面的移动。这些结果表明，etoh变性β-甘氨酸和甘氨酸参与了HHP处理过程中结构变化的不同途径。
The effects of high hydrostatic pressure (HHP) treatment (100-500 MPa) on solubility and structural properties of ethanol (EtOH)-denatured soy β-conglycinin and glycinin were investigated using differential scanning calorimetry, Fourier transform infrared and ultraviolet spectroscopy. HHP treatment above 200 MPa, especially at neutral and alkaline pH as well as low ionic strength, significantly improved the solubility of denatured soy proteins. Structural rearrangements of denatured β-conglycinin subjected to high pressure were confirmed, as evidenced by the increase in enthalpy value (ΔH) and the formation of the ordered supramolecular structure with stronger intramolecular hydrogen bond. HHP treatment (200-400 MPa) caused an increase in surface hydrophobicity (F(max)) of β-conglycinin, partially attributable to the exposure of the Tyr and Phe residues, whereas higher pressure (500 MPa) induced the decrease in F(max) due to hydrophobic rearrangements. The Trp residues in β-conglycinin gradually transferred into a hydrophobic environment, which might further support the finding of structural rearrangements. In contrast, increasing pressure induced the progressive unfolding of denatured glycinin, accompanied by the movement of the Tyr and Phe residues to the molecular surface of protein. These results suggested that EtOH-denatured β-conglycinin and glycinin were involved in different pathways of structural changes during HHP treatment.