论文部分内容阅读
A series of soy protein isolate (SPI) films plasticized by glycerol (Gly) were studied using attenua ted total reflectance-Fourier transform infrared spectroscopy (ATR/FTIR).Perturbation-correlation moving window two-dimensional (PCMW2D) and two-dimensional correlation (2DCOS) analyses were applied to the amide Ⅰ band and thus the hydrogen bond interaction between SPI and Gly was systematically investigated.When Gly concentrations were in the range 0~35%, the hydrogen bond among β-sheets was replaced by the one between SPI chain and Gly molecule, which caused these protein chains being changed to α-helix.Howev er, the transformation of β-sheet to α-helix was saturated and both of them tend to change to random coil when Gly concentrations were in the range 35%~60%.