FOOD SCIENCE ›› 2012, Vol. 33 ›› Issue (9): 54-57.doi: 10.7506/spkx1002-6630-201209012

• Basic Research • Previous Articles     Next Articles

Relationship between Structure and Surface Hydrophobicity of Soybean Protein Isolates from Different Varieties

WANG Chen1，JIANG Lian-zhou1,2,*，WEI Dong-xu1,3，LI Yang1，SUI Xiao-nan1，WANG Zhong-jiang1,2，LI Dan1,4   

  1. (1. College of Food Science, Northeast Agricultural University, Harbin 150030, China；2. National Research Center of Soybean Engineering and Technology, Harbin 150030, China；3. Heilongjiang Entry-Exit Inspect and Quarantine Bureau, Harbin 150001, China；4. Department of Biological Engeering, Ningde Normal University, Ningde 352100, China)
  • Online:2012-05-15 Published:2012-05-07

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Abstract: FTIR (fourier transform infra-red spectroscopy) was applied to explore the secondary structure of soybean protein isolates from different varieties. The overlapped peaks of amide Ⅰof soy protein isolates from different species could be fitted by Gauss peak to reveal the characteristic peaks ofα-helix, β-sheet, β-turn and random coil. Their contents and surface hydrophobicity were determined to explore the structure-activity relationship of soybean protein isolates. The results revealed a good negative correlation between the surface hydrophobicity and α-helix content (r ＝－0.945, P ＝ 0.004), and a positive correlation between the surface hydrophobicity and β-sheet (r ＝ 0.904, P ＝ 0.013) or random coil content (r ＝ 0.866, P ＝0.026). No significant correlation between β-turn and the surface hydrophobicity (r ＝－0.698, P ＝ 0.123).

Key words: soybean protein isolate, FTIR, surface hydrophobicity

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