Surface hydrophobicity (SH) properties of the trimeric storage protein phaseolin (black gram phaseolin [BGP]) of black gram (Vigna mungo) were investigated using 8-anilinonaphthalene-1-sulfonate (ANS) as an extrinsic fluorescent probe. The emission maxima of fluorescence spectra of BGP:ANS complex were blue-shifted to 455 nm as compared to 515 nm for the free ANS. Saturation binding occurred at a dye-to-protein ratio of about 30:1. The quantum yield of the complex increased with increasing ionic strength. The Kd values were 1.7 × 10-5 and 1.37 × 10-5 M using fractional occupancy and Scatchard analysis, respectively. Analysis of the binding data using Klotz plot revealed 4 binding sites/protomer. SH of BGP was 48%, which rapidly decreased due to the perturbation of the binding sites as the protein unfolded in GdnHCl and urea. By varying processing conditions, it may be possible to alter the surface exposure of SH of BGP to extend its applications in novel food products with desired textural attributes.
Practical application: Varying solvent and/or processing conditions can assist to modulate the surface hydrophobicity of functional legume proteins to achieve desired textural properties in the end product.
Keywords: black gram; hydrophobicity; phaseolin; protein.
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