Journal of Jilin University Science Edition

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Analysis of Soy Glycinin by FTIR and Raman Spectroscopy

LONG Guohui1, JI Yuan2, PAN Hongbin3,4, SUN Zewei4, WANG Jinxin1, QIN Guixin4   

  1. 1. College of Life Science, Jilin Agricultural University, Changchun 130118, China; 2. College of Physics, Jilin University, Changchun 130012, China; 3. Key Laboratory of Animal Nutritionand Feed of Yunnan Province, Yunan Agricultural University, Kunming 650201, China;4. College of Animal Science and Technology, Jilin Agricultural University, Changchun 130118, China
  • Received:2013-10-15 Online:2014-07-26 Published:2014-09-26
  • Contact: QIN Guixin E-mail:qgx2013@sohu.com

Abstract:

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 ass
essed by the deconvolution amide Ⅰ band and curvefitting. Quantitative analysis of secondary structure reveals that the results of the folded glycinin β
sheet had no significant difference, while the glycinin α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 (11.1%) 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.

Key words: molecular structure, FTIR, Raman spectroscopy, glycinin

CLC Number: 

  • Q512