CAJ | 학술논문

利用 Fourier 变换红外光谱(FTIR)和激光 Raman 光谱研究大豆球蛋白的结构,并对大豆球蛋白的红外光谱和 Raman 光谱的特征峰进行指认,计算 Raman 费米共振 I 850/830的比值.结果表明：红外光谱和 Raman 光谱的酰胺Ⅰ带去卷积和曲线拟合获得二级结构,其中β-折叠结果差异较小,α-螺旋、β-转角和无规卷曲结果差异较大(p <0.05)；红外光谱在1618,1682 cm-1处的吸收峰归属于大豆球蛋白的分子间和分子内聚集,拟合峰面积百分数分别为11.1%和9.5%；包埋和外露的酪氨酸残基占酪氨酸残基总量的14%和86%.
이용 Fourier 변환홍외광보(FTIR)화격광 Raman 광보연구대두구단백적결구,병대대두구단백적홍외광보화 Raman 광보적특정봉진행지인,계산 Raman 비미공진 I 850/830적비치.결과표명：홍외광보화 Raman 광보적선알Ⅰ대거권적화곡선의합획득이급결구,기중β-절첩결과차이교소,α-라선、β-전각화무규권곡결과차이교대(p <0.05)；홍외광보재1618,1682 cm-1처적흡수봉귀속우대두구단백적분자간화분자내취집,의합봉면적백분수분별위11.1%화9.5%；포매화외로적락안산잔기점락안산잔기총량적14%화86%.
The molecular structure of glycinin was investigated by FTIR and Raman spectroscopy.The frequency and signal intensity of IR and Raman bands were assigned.The data suggest that FTIR and Raman spectra reflect a large amount of structural information.The secondary structure of glycinin was assessed by the deconvolution amide Ⅰ band and curve-fitting.Quantitative analysis of secondary structure reveals that the results of the folded glycininβ-sheet had no significant difference,while the glycininα-helix,turning angle,random coil had significant difference (p <0.05).The IR bands at 1 618 cm-1 and 1 682 cm-1 were considered to reflect the formation of intermolecular aggregates (1 1.1%)and intramolecular aggregates (9.5%).The I 850/830 intensity ratio of Raman tyrosine doublet suggests that the contents of the buried tyrosine residue and exposed tyrosine residue were 14% and 86% in glycinin.