Development of Novel Nanocarriers by Ultrasound and Ethanol-Assisted Soy Protein Isolate: Enhancing the Resistance of Lutein to Environmental Stress
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...
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Veröffentlicht in: | Journal of agricultural and food chemistry 2024-03, Vol.72 (11), p.5912-5925 |
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container_title | Journal of agricultural and food chemistry |
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creator | Cheng, Xiaoyi Meng, Fanda Lou, Muyu Peng, Ruiqi Zou, Mingxi Zhang, Hezhen Wu, Yi Wang, Huan Xu, Jing Jiang, Lianzhou |
description | 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 (H 0 = 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. |
doi_str_mv | 10.1021/acs.jafc.3c09415 |
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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 (H 0 = 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. 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Agric. Food Chem</addtitle><description>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 (H 0 = 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. 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Agric. Food Chem</addtitle><date>2024-03-20</date><risdate>2024</risdate><volume>72</volume><issue>11</issue><spage>5912</spage><epage>5925</epage><pages>5912-5925</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><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 (H 0 = 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.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>38446598</pmid><doi>10.1021/acs.jafc.3c09415</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0002-5200-1166</orcidid></addata></record> |
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title | Development of Novel Nanocarriers by Ultrasound and Ethanol-Assisted Soy Protein Isolate: Enhancing the Resistance of Lutein to Environmental Stress |
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