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Development of Novel Nanocarriers by Ultrasound and Ethanol-Assisted Soy Protein Isolate: Enhancing the Resistance of Lutein to Environmental Stress.
Cheng, Xiaoyi; Meng, Fanda; Lou, Muyu; Peng, Ruiqi; Zou, Mingxi; Zhang, Hezhen; Wu, Yi; Wang, Huan; Xu, Jing; Jiang, Lianzhou.
Affiliation
  • Cheng X; College of Arts and Sciences, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
  • Meng F; College of Arts and Sciences, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
  • Lou M; College of Arts and Sciences, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
  • Peng R; College of Arts and Sciences, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
  • Zou M; College of Arts and Sciences, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
  • Zhang H; College of Arts and Sciences, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
  • Wu Y; College of Arts and Sciences, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
  • Wang H; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
  • Xu J; College of Arts and Sciences, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
  • Jiang L; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
J Agric Food Chem ; 72(11): 5912-5925, 2024 Mar 20.
Article in En | MEDLINE | ID: mdl-38446598
ABSTRACT
The aim of this work was to investigate the effects of the processing sequence of ultrasound and ethanol on the physicochemical properties of soy protein isolate (SPI), which were further evaluated for the morphology and stability of SPI-lutein coassembled nanoparticles. The results showed that the sequence of ultrasound followed by ethanol treatment was the optimal one. The samples were subjected to ultrasonication followed by subunit disassembly and reassembly induced by 40% (v/v) ethanol, with the resulting molecular unfolding and subsequent aggregation being attributed to intramolecular hydrogen bonds. The recombined nanoparticles had smaller particle size (142.43 ± 2.91 nm) and turbidity (0.16 ± 0.01), and the exposure of more hydrophobic groups (H0 = 6221.00 ± 130.20) induced a shift of SPI structure toward a more ordered direction. The homogeneous and stable particle provided excellent stability for the loading of lutein. The bioaccessibility (from 25.48 ± 2.35 to 65.85 ± 1.78%) and release rate of lutein were modulated in gastrointestinal digestion experiments. Our discoveries provide a new perspective for the development of combined physicochemical modification of proteins as nanocarriers in functional foods.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Lutein / Soybean Proteins Language: En Journal: J Agric Food Chem Year: 2024 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Lutein / Soybean Proteins Language: En Journal: J Agric Food Chem Year: 2024 Document type: Article Affiliation country:
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