Improved Light and In Vitro Digestive Stability of Lutein-Loaded Nanoparticles Based on Soy Protein Hydrolysates via Pepsin

Renyi Wu; Xuejiao Qie; Zhaojun Wang; Qiuming Chen; Maomao Zeng; Jie Chen; Fang Qin; Zhiyong He

doi:10.3390/foods11223635

Improved Light and In Vitro Digestive Stability of Lutein-Loaded Nanoparticles Based on Soy Protein Hydrolysates via Pepsin

Foods. 2022 Nov 14;11(22):3635. doi: 10.3390/foods11223635.

Authors

Renyi Wu^{1

2}, Xuejiao Qie^{1

2}, Zhaojun Wang^{1

2}, Qiuming Chen^{1

2}, Maomao Zeng^{1

2}, Jie Chen^{1

2}, Fang Qin^{1

2}, Zhiyong He^{1

2}

Affiliations

¹ State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
² International Joint Laboratory on Food Safety, Jiangnan University, Wuxi 214122, China.

Abstract

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.

Keywords: encapsulation; lutein; nanoparticles; soy protein hydrolysates; stability.

Abstract

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