Insights Into Interaction of Lutein with Pea Protein Isolate in Aqueous Nanometre-Scale Dispersion: Thermal Stability, Spectroscopic, and Morphological Properties

IF 2.8 4区农林科学 Q2 FOOD SCIENCE & TECHNOLOGY

Food Biophysics Pub Date : 2024-11-21 DOI:10.1007/s11483-024-09904-z

Yuanyuan Li, Baoyi Wang, Qingyan Li, Xuefang Hu, Xiuqing Zhang, Haisheng Pei

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Abstract

Attaining an appropriate color is a pivotal factor in achieving a desirable appearance for pea-based products. Although the color of lutein is vibrant, its stability during thermal processing remains a significant challenge that has yet to be overcome. A comprehensive understanding of the interactions between pea protein isolate (PPI) and lutein, as well as their influence on lutein retention and the solution behavior of PPI itself, is crucial for the development of pea protein-based products with optimized color. Currently, PPI provided a pronounced protective effect against the thermal degradation of lutein, primarily by influencing the retention rate, overall color variation, and total antioxidant capacity of lutein. Fluorescence spectroscopy revealed static quenching with strong affinity between PPI and lutein. The surface hydrophobicity of PPI after binding lutein decreased significantly (p < 0.05), while the secondary structure of PPI remained stable without notable relaxation or unfolding. Notably, lutein exists in both dispersed and aggregated forms, while the resulting lutein–PPI complex manifested as stable spherical nanoparticles. Polydispersity index and Z-average diameter measurements reveal that the lutein–PPI complex is more homogeneous and stable than PPI alone. In summary, compared to previous references, the present study fundamentally enhanced understanding of the underlying mechanisms involved in the interaction of PPI with lutein, thereby providing valuable insights for the development of novel plant-derived protein products with improved color stability.

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深入了解叶黄素与豌豆蛋白隔离物在纳米级水分散体中的相互作用：热稳定性、光谱和形态特性

获得适当的色泽是豌豆产品获得理想外观的关键因素。虽然叶黄素的颜色鲜艳，但其在热加工过程中的稳定性仍然是一个有待克服的重大挑战。全面了解豌豆蛋白分离物（PPI）和叶黄素之间的相互作用，以及它们对叶黄素保留和 PPI 本身溶液行为的影响，对于开发具有最佳色泽的豌豆蛋白产品至关重要。目前，PPI 对叶黄素的热降解具有明显的保护作用，主要是通过影响叶黄素的保留率、整体颜色变化和总抗氧化能力。荧光光谱显示，PPI 与叶黄素之间具有强亲和力的静态淬灭作用。与叶黄素结合后，PPI 的表面疏水性明显降低（p < 0.05），而 PPI 的二级结构保持稳定，没有明显的松弛或解折。值得注意的是，叶黄素以分散和聚集两种形式存在，而由此产生的叶黄素-PPI 复合物则表现为稳定的球形纳米颗粒。多分散指数和 Z 平均直径测量结果表明，叶黄素-PPI 复合物比单独的 PPI 更均匀、更稳定。总之，与之前的参考文献相比，本研究从根本上加深了人们对 PPI 与叶黄素相互作用的内在机制的理解，从而为开发具有更好颜色稳定性的新型植物源蛋白质产品提供了宝贵的见解。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Food Biophysics 工程技术-食品科技

CiteScore

5.80

自引率

3.30%

发文量

审稿时长

1 months

期刊介绍： Biophysical studies of foods and agricultural products involve research at the interface of chemistry, biology, and engineering, as well as the new interdisciplinary areas of materials science and nanotechnology. Such studies include but are certainly not limited to research in the following areas: the structure of food molecules, biopolymers, and biomaterials on the molecular, microscopic, and mesoscopic scales; the molecular basis of structure generation and maintenance in specific foods, feeds, food processing operations, and agricultural products; the mechanisms of microbial growth, death and antimicrobial action; structure/function relationships in food and agricultural biopolymers; novel biophysical techniques (spectroscopic, microscopic, thermal, rheological, etc.) for structural and dynamical characterization of food and agricultural materials and products; the properties of amorphous biomaterials and their influence on chemical reaction rate, microbial growth, or sensory properties; and molecular mechanisms of taste and smell. A hallmark of such research is a dependence on various methods of instrumental analysis that provide information on the molecular level, on various physical and chemical theories used to understand the interrelations among biological molecules, and an attempt to relate macroscopic chemical and physical properties and biological functions to the molecular structure and microscopic organization of the biological material.