...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>LWT-Food Science & Technology >Mechanistic study on the nanocomplexation between curcumin and protein hydrolysates from Great Northern bean (Phaseolus vulgaris L.) for delivery applications in functional foods
【24h】

Mechanistic study on the nanocomplexation between curcumin and protein hydrolysates from Great Northern bean (Phaseolus vulgaris L.) for delivery applications in functional foods

机译：从北部豆豆（PHEAPOLUSULUS L.）姜黄素和蛋白质水解产物的纳米复合物的机械研究在功能性食品中的输送应用

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

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 mu m in diameter), self-assembled nanocomplexation took place spontaneously after mixing with curcumin, with size ranging from 244.7 to 344.7 nm. BPH with 5% degree of hydrolysis (DH) showed the highest curcumin loading capacity value (9.97 mu g/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 mu g/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.
机译：利用植物蛋白，如干食用豆（Phaseolus vulgaris L.）蛋白，作为经济高效的生物材料，取代动物蛋白，在食品中输送营养素，已经引起了人们极大的兴趣。通过调节酶解程度，可以进一步改善大豆蛋白的功能特性。在本研究中，研究了大北方豆水解物（BPH）与姜黄素的络合作用。与微米级的BPH球蛋白（直径1.2-1.5μm）相比，与姜黄素混合后，自组装纳米复合物自发发生，大小在244.7-344.7 nm之间。水解度（DH）为5%的BPH表现出最高的姜黄素载量值（9.97μg/mg）。通过研究固有荧光猝灭和姜黄素荧光增强，我们发现，与原始蛋白质相比，低DH时结合亲和力增加，但在7%或更高DH时结合亲和力降低。BPH-5表现出最高的负载能力（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。本研究的发现为功能性食品中基于植物蛋白的递送系统的制作、优化和选择提供了见解。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号