FOOD SCIENCE ›› 2012, Vol. 33 ›› Issue (11): 47-51.doi: 10.7506/spkx1002-6630-201211011

• Basic Research • Previous Articles     Next Articles

Effect of pH on Conformation and Surface Hydrophobicity of Soybean Protein Isolate

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

  1. (1. College of Food Science, Northeast Agricultural University, Harbin 150030, China;2. National Soybean Engineering Technology Research Center, Harbin 150030, China;3. Heilongjiang Entry-Exit Inspection and Quarantine Bureau, Harbin 150001, China; 4. Ningde Normal University, Ningde 352100, China)
  • Online:2012-06-15 Published:2012-07-27

Abstract: Lowry method, ANS fluorescence probe, circular dichroism and fluorescent spectroscopy were applied to explore the solubility, surface hydrophobicity, secondary structure and tertiary structure of soybean protein isolate at different pH conditions. The results showed that the transformation from β-sheet structure to α-helix structure, and the microenvironment polarity of Trp residues revealed an obvious increase with increasing pH. A negatively linear correlation between the surface hydrophobicity and solubility of soybean protein isolate was observed. Meanwhile, the surface hydrophobicity of soybean protein isolate was negatively correlated with the amount of α-helix structure.

Key words: soybean protein isolate, pH, hydrophobicity, structure

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