CAJ | 학술논문

采用转矩流变仪在30℃和90℃对含水60％的大豆分离蛋白分别处理2 min，15 min，30 min，考察其FT-IR光谱特性的变化。实验结果表明，热-机械处理导致大豆分离蛋白分子的-CH2中的C-H对称及非对称伸缩减弱甚至消失，C-H伸缩振动和非对称伸缩向高位漂移，蛋白二级结构中α-螺旋和β-转角含量降低，同时伴有β-折叠和无规则卷曲含量升高。对于低水分大豆分离蛋白体系，热-机械处理中的机械效应可能是导致其蛋白二级结构变化的主要因素。
채용전구류변의재30℃화90℃대함수60％적대두분리단백분별처리2 min，15 min，30 min，고찰기FT-IR광보특성적변화。실험결과표명，열-궤계처리도치대두분리단백분자적-CH2중적C-H대칭급비대칭신축감약심지소실，C-H신축진동화비대칭신축향고위표이，단백이급결구중α-라선화β-전각함량강저，동시반유β-절첩화무규칙권곡함량승고。대우저수분대두분리단백체계，열-궤계처리중적궤계효응가능시도치기단백이급결구변화적주요인소。
Soybean protein isolate(SPI)with a moisture content of 60% was thermo-mechanically treated torque rheometer at 30 ℃and 90 ℃for 2 min,1 5 min and 30 min respectively,and characterized by Fou-rier transform infrared (FT-IR)spectroscopy.The results showed that after thermo-mechanical treatments, the symmetrical and asymmetrical stretching of C-H bonds in -CH2 resides became weak and even dis-appeared the stretching vibration and asymmetrical stretching of C-H bonds drifted to higher position.The α-helix andβ-turn decreased accompanying withβ-sheet and random coil increased.For that lower moisture content SPI system,the mechanical effect during thermo-mechanical processing may be the major contribu-tor to the transformation of secondary protein structure.