叶黄素
化学
大豆蛋白
荧光光谱法
胃蛋白酶
食品科学
生物化学
类胡萝卜素
荧光
酶
量子力学
物理
作者
Renyi Wu,Xuejiao Qie,Zhaojun Wang,Qiuming Chen,Maomao Zeng,Jie Chen,Fang Qin,Zhiyong He
出处
期刊:Foods
[MDPI AG]
日期:2022-11-14
卷期号:11 (22): 3635-3635
标识
DOI:10.3390/foods11223635
摘要
In order to improve the water solubility and stability of lutein, soy protein isolates (SPI) and their hydrolysates via pepsin (PSPI) and alcalase (ASPI) were used as nanocarriers for lutein to fabricate the lutein-loaded nanoparticles (LNPS) of SPI, PSPI, and ASPI. The encapsulation properties, light, and in vitro digestive stability of lutein in nanoparticles, and protein–lutein interactions were investigated. Compared with SPI-LNPS and ASPI-LNPS, PSPI-LNPS was characterized by uniform morphology (approximately 115 nm) with a lower polydispersity index (approximately 0.11) and higher lutein loading capacity (17.96 μg/mg protein). In addition, PSPI-LNPS presented the higher lutein retention rate after light exposure (85.05%) and simulated digestion (77.73%) than the unencapsulated lutein and SPI-LNPS. Fluorescence spectroscopy revealed that PSPI had stronger hydrophobic interaction with lutein than SPI, which positively correlated with their beneficial effects on the light and digestive stability of lutein. This study demonstrated that PSPI possessed significant potential for lutein delivery.
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