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中文摘要：
采用傅里叶转换红外光谱技术（FTIR）研究了高压（HP）处理对冷冻干燥的大豆分离蛋白（SPI）构象的影响。在SPI的去卷积FTIR光谱的酰胺Ⅰ′区域（1600～1700cm^-1）,观察到12个与蛋白构象相关的红外吸收峰,分别对应于CO键伸缩振动与肽键的C—N伸缩振动。通过对该区域的峰强度与波数分析显示,压力为200～400MPa的HP处理导致SPI在该区域的峰发生明显的“红移”（约2cm^-1）,强度也显著增加。更高的HP处理进一步增强了SPI的酰胺Ⅰ′区域的峰强度。对酰胺Ⅱ峰分析显示,HP处理导致酰胺Ⅱ峰（如1560～1500cm^-1）的强度、面积逐渐增加（与压力呈正相关）。以上分析显示,HP处理导致SPI的二级与三级结构逐渐打开,然而变性蛋白的结构在高压释放后经历一个“重构过程”。
英文摘要：
The effect of high pressure （HP）treatment on the conformation of freeze-dried soy protein isolates （SPI）was investigated by Fourier transform infrared （FTIR） spectroscopy. Within the amide Ⅰ ＇ region （1 600-1 700 cm^-1 ）of the deeonvoluted FTIR curve of SPI, more than 10 bands associated with protein conformation were distinctly observed, attributed to the C=O stretching vibration and to a small extent to C-N stretching vibration of the peptide bonds, respectively. The secondary structure of native SPI is estimated to be composed of 15%-16% α-helix, 39%-44% extended strands, 17. 5% random coils, and 21%-27 % turns. The analyses of intensity and wavenumber of the bands showed that, HP treatment at pressures of 200-400 MPa resulted in the increases in intensity and a ＂red-shift＂ （about 2 cm^-1 ）of these bands. HP treatment at 600 MPa further increased the band intensity of the amide Ⅰ ＇ region. The analyses of amide II bands showed that HP treatment led to gradual increases in intensity and absolute area of amide Ⅱ bands, in a pressure-dependent manner. Thus, it is suggested that HP treatment resulted in gradual unfolding of secondary and tertiary structure of SPI, while the structure of denatured proteins underwent a ＂rebuilding＂ process after the release of high pressure. These results confirm that the HP-induced modification of SPI is by means of the HP-induced conformational changes.
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