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.

中文翻译：

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与 8-Anilinonaphthalene-1-Sulfoniac Acid (ANS) 的相互作用和黑革兰 (Vigna mungo) 菜豆素的表面疏水性

使用 8-anilinonaphthalene-1-sulfonate (ANS) 作为外在荧光探针研究了黑克 (Vigna mungo) 三聚体储存蛋白菜豆蛋白 (黑克菜豆蛋白 [BGP]) 的表面疏水性 (SH) 特性。与游离 ANS 的 515 nm 相比，BGP:ANS 复合物的荧光光谱发射最大值蓝移至 455 nm。饱和结合发生在约 30:1 的染料与蛋白质的比率下。配合物的量子产率随着离子强度的增加而增加。使用分数占用率和 Scatchard 分析，Kd 值分别为 1.7 × 10-5 和 1.37 × 10-5 M。使用 Klotz 图分析结合数据揭示了 4 个结合位点/原体。BGP 的 SH 为 48%，由于蛋白质在 GdnHCl 和尿素中展开时结合位点的扰动而迅速下降。通过改变加工条件，可以改变 BGP SH 的表面暴露，以扩展其在具有所需质地属性的新型食品中的应用。实际应用 不同的溶剂和/或加工条件有助于调节功能性豆科植物蛋白的表面疏水性，从而在最终产品中获得所需的质地特性。