Formation of pea protein amyloid fibrils to stabilize high internal phase emulsions for encapsulation of lutein

Formation of pea protein amyloid fibrils to stabilize high internal phase emulsions for encapsulation of lutein
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形成豌豆蛋白淀粉样原纤维以稳定高内相乳液以封装叶黄素

DOI:
10.1016/j.jff.2022.105110
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发表时间:
2022-07
影响因子:
5.6
通讯作者:
Bing Hu
Bing Hu
中科院分区:
农林科学2区
文献类型:
--
作者:
Huaqian Wu;Yingqun Nian;Yanhua Liu;Yeyang Zhang;Bing Hu

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• Pea protein formed fibrils with polymorphism via hydrolysis and re-assembly. • Pea protein fibrils stabilized HIPEs with internal phase volume fraction upto 90%. • HIPEs was enhanced with increase of fibril content and mixing dispersion speed. • Typical microstructure of highly packed polyhedral geometric oil droplets appeared. • The HIPEs encapsulated lutein and improved its stability against UV, heat and Fe 3+ . Thermal treatment of purified pea protein in acidic environment was found to induce the hydrolysis and re-assembly of the protein to form amyloid fibrils. Pea protein amyloid fibrils showed high polymorphism with the coexistence of mature and worm-like fibrils. Pea protein amyloid fibrils can stabilize the high internal phase emulsions (HIPEs) with the internal phase volume fraction as high as 90%. The gel strength of HIPEs was enhanced with the increase of pea protein amyloid fibril contents and the dispersion speed. The typical microstructure of highly packed polyhedral geometric oil droplets appeared in both the laser scanning confocal microscopy (CLSM) and Cryo-scan electron microscopy (Cryo-SEM) images of the HIPEs samples. High loading content of lutein upto 0.2 wt% in the prepared HIPEs was realized and the stability of lutein against ultraviolet irradiation, heat and iron was promoted significantly.
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