There has been a great interest in utilization of plant protein such as dry edible bean (Phaseolus vulgaris L.) proteins as cost-effective biomaterials to replace animal proteins for delivery of nutrients in foods. The functional properties of bean proteins may be further improved by tuning the degree of enzymatic hydrolysis. In this study, the complexation of Great Northern bean hydrolysates (BPH) with curcumin was investigated. Compared to the micro-sized BPH globulins (1.2-1.5 μm in diameter), self-assembled nanocomplexation took place spontaneously after mixing with curcumin, with size ranging from 244.7-344.7 nm. BPH with 5% degree of hydrolysis (DH) showed the highest curcumin loading capacity value (9.97 μg/mg). By investigating the intrinsic fluorescence quenching and curcumin fluorescence enhancement, we found that the binding affinity was increased at low DH but decreased at the DH of 7% or higher, compared to pristine protein. BPH-5 showed the highest loading capacity (9.97 μg/mg), relatively small particle size (286.9 nm) and low PDI value (0.359), and optimal storage stability, which was mainly attributed to its relatively high binding affinity and surface hydrophobicity. The findings in this study provide insight on fabricating, optimizing and selecting plant protein-based delivery systems in functional foods.

人们对利用植物蛋白如干食用豆（菜豆）有极大的兴趣。L.）蛋白是一种具有成本效益的生物材料，可以代替动物蛋白在食物中输送营养。豆蛋白的功能特性可通过调节酶促水解程度来进一步改善。在这项研究中，研究了大黄豆水解物（BPH）与姜黄素的络合作用。与微米大小的BPH球蛋白（直径为1.2-1.5μm）相比，自组装纳米复合物在与姜黄素混合后会自发发生，大小范围为244.7-344.7 nm。具有5％水解度（DH）的BPH表现出最高的姜黄素负载量值（9.97μg/ mg）。通过研究固有的荧光猝灭和姜黄素荧光增强，我们发现与原始蛋白质相比，结合亲和力在低DH时增加，但在DH 7％或更高时降低。BPH-5表现出最高的负载量（9.97μg/ mg），相对较小的粒径（286.9 nm）和较低的PDI值（0.359），以及最佳的储存稳定性，这主要归因于其相对较高的结合亲和力和表面疏水性。这项研究的发现为功能性食品的制造，优化和选择基于植物蛋白的传递系统提供了见识。