Influence of pH on Structure and Surface Hydrophobicity of Glycinin

doi:10.7506/spkx1002-6630-201511001

Abstract

Abstract:

Lowry method, 8-anilinonaphthalene-1-sulfonic acid ammonium salt (ANS) fluorescence probe, circular
dichroism and fluorescence spectroscopy were applied to explore the solubility, surface hydrophobicity, secondary structure
and tertiary structure of glycinin at different pH conditions with the aim to provide the theoretical basis for the research on
relationship between soybean protein structure and surface hydrophobicity. The results showed that the transformation from
β-sheet structure and random coil to α-helix structure occurred, and the microenvironment polarity of Trp residues revealed
an obvious decrease with increasing pH. A negatively linear correlation between the surface hydrophobicity and solubility
of glycinin was observed, and the surface hydrophobicity of glycinin was also negatively correlated with the content of
α-helix structure.

Key words: glycinin, pH, structure, surface hydrophobicity

CLC Number:

TS201.2

WEI Dongxu1,2, JIANG Lianzhou1,*, WANG Chen3, WANG Zhongjiang1. Influence of pH on Structure and Surface Hydrophobicity of Glycinin[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201511001.

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Influence of pH on Structure and Surface Hydrophobicity of Glycinin

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