Improvement of physicochemical properties of lycopene by the self‐assembly encapsulation of recombinant ferritin GF1 from oyster ( Crassostrea gigas)

Abstract BACKGROUND Lycopene (LYC), a carotenoid found in abundance in ripe red fruits, exhibits higher singlet oxygen quenching activity than other carotenoids. However, the stability of LYC is extremely poor due to its high double‐bond content. In this paper, a nano‐encapsulation strategy based on...

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Published in:Journal of the Science of Food and Agriculture
Main Authors: Xia, Xiaoyu, Li, Han, Xu, Xianbing, Wu, Chao, Wang, Zhenyu, Zhao, Guanghua, Du, Ming
Other Authors: National Natural Science Foundation of China
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2024
Subjects:
Online Access:http://dx.doi.org/10.1002/jsfa.13163
https://onlinelibrary.wiley.com/doi/pdf/10.1002/jsfa.13163
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spelling crwiley:10.1002/jsfa.13163 2024-06-02T08:05:38+00:00 Improvement of physicochemical properties of lycopene by the self‐assembly encapsulation of recombinant ferritin GF1 from oyster ( Crassostrea gigas) Xia, Xiaoyu Li, Han Xu, Xianbing Wu, Chao Wang, Zhenyu Zhao, Guanghua Du, Ming National Natural Science Foundation of China 2024 http://dx.doi.org/10.1002/jsfa.13163 https://onlinelibrary.wiley.com/doi/pdf/10.1002/jsfa.13163 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Journal of the Science of Food and Agriculture volume 104, issue 5, page 2783-2791 ISSN 0022-5142 1097-0010 journal-article 2024 crwiley https://doi.org/10.1002/jsfa.13163 2024-05-03T11:38:56Z Abstract BACKGROUND Lycopene (LYC), a carotenoid found in abundance in ripe red fruits, exhibits higher singlet oxygen quenching activity than other carotenoids. However, the stability of LYC is extremely poor due to its high double‐bond content. In this paper, a nano‐encapsulation strategy based on highly stable marine‐derived ferritin GF1 nanocages was used to improve the thermal stability and oxidation resistance of LYC, thereby boosting its functional effectiveness and industrial applicability. RESULTS The preparation of GF1‐LYC nanoparticles benefited from the pH‐responsive reversible self‐assembly of GF1 to capture LYC molecules into GF1 cavities with a LYC‐to‐protein ratio of 51 to 1. After the encapsulation of the LYC, the reassembled GF1 nanocages maintained intact morphology and good monodispersity. The GF1‐LYC nanoparticles incorporated the characteristic LYC peaks in spectrograms, and their powder form contained the crystalline form of LYC. Molecular docking revealed that LYC bound with the inner triple‐axis channel areas of GF1, interacting with VAL139, LYS72, LYS65, TYR69, PHE129, HIS133, HIS62, and TYR134 amino acids through hydrophobic bonds. Fourier transform infrared spectroscopy also demonstrated the bonding of GF1 and LYC. In comparison with free LYC, GF1 reduced the thermal degradation of encapsulated LYC at 37 °C significantly and maintained the 2,2‐Diphenyl‐1‐picrylhydrazyl (DPPH)‐scavenging ability of LYC. CONCLUSION As expected, the water solubility, thermal stability, and antioxidant capacity of encapsulated LYC from GF1‐LYC nanoparticles was notably improved in comparison with free LYC, indicating that the shell‐like marine ferritin nanoplatform might enhance the stable delivery of LYC and promote its utilization in the field of food nutrition and in other industries. © 2023 Society of Chemical Industry. Article in Journal/Newspaper Crassostrea gigas Wiley Online Library Journal of the Science of Food and Agriculture 104 5 2783 2791
institution Open Polar
collection Wiley Online Library
op_collection_id crwiley
language English
description Abstract BACKGROUND Lycopene (LYC), a carotenoid found in abundance in ripe red fruits, exhibits higher singlet oxygen quenching activity than other carotenoids. However, the stability of LYC is extremely poor due to its high double‐bond content. In this paper, a nano‐encapsulation strategy based on highly stable marine‐derived ferritin GF1 nanocages was used to improve the thermal stability and oxidation resistance of LYC, thereby boosting its functional effectiveness and industrial applicability. RESULTS The preparation of GF1‐LYC nanoparticles benefited from the pH‐responsive reversible self‐assembly of GF1 to capture LYC molecules into GF1 cavities with a LYC‐to‐protein ratio of 51 to 1. After the encapsulation of the LYC, the reassembled GF1 nanocages maintained intact morphology and good monodispersity. The GF1‐LYC nanoparticles incorporated the characteristic LYC peaks in spectrograms, and their powder form contained the crystalline form of LYC. Molecular docking revealed that LYC bound with the inner triple‐axis channel areas of GF1, interacting with VAL139, LYS72, LYS65, TYR69, PHE129, HIS133, HIS62, and TYR134 amino acids through hydrophobic bonds. Fourier transform infrared spectroscopy also demonstrated the bonding of GF1 and LYC. In comparison with free LYC, GF1 reduced the thermal degradation of encapsulated LYC at 37 °C significantly and maintained the 2,2‐Diphenyl‐1‐picrylhydrazyl (DPPH)‐scavenging ability of LYC. CONCLUSION As expected, the water solubility, thermal stability, and antioxidant capacity of encapsulated LYC from GF1‐LYC nanoparticles was notably improved in comparison with free LYC, indicating that the shell‐like marine ferritin nanoplatform might enhance the stable delivery of LYC and promote its utilization in the field of food nutrition and in other industries. © 2023 Society of Chemical Industry.
author2 National Natural Science Foundation of China
format Article in Journal/Newspaper
author Xia, Xiaoyu
Li, Han
Xu, Xianbing
Wu, Chao
Wang, Zhenyu
Zhao, Guanghua
Du, Ming
spellingShingle Xia, Xiaoyu
Li, Han
Xu, Xianbing
Wu, Chao
Wang, Zhenyu
Zhao, Guanghua
Du, Ming
Improvement of physicochemical properties of lycopene by the self‐assembly encapsulation of recombinant ferritin GF1 from oyster ( Crassostrea gigas)
author_facet Xia, Xiaoyu
Li, Han
Xu, Xianbing
Wu, Chao
Wang, Zhenyu
Zhao, Guanghua
Du, Ming
author_sort Xia, Xiaoyu
title Improvement of physicochemical properties of lycopene by the self‐assembly encapsulation of recombinant ferritin GF1 from oyster ( Crassostrea gigas)
title_short Improvement of physicochemical properties of lycopene by the self‐assembly encapsulation of recombinant ferritin GF1 from oyster ( Crassostrea gigas)
title_full Improvement of physicochemical properties of lycopene by the self‐assembly encapsulation of recombinant ferritin GF1 from oyster ( Crassostrea gigas)
title_fullStr Improvement of physicochemical properties of lycopene by the self‐assembly encapsulation of recombinant ferritin GF1 from oyster ( Crassostrea gigas)
title_full_unstemmed Improvement of physicochemical properties of lycopene by the self‐assembly encapsulation of recombinant ferritin GF1 from oyster ( Crassostrea gigas)
title_sort improvement of physicochemical properties of lycopene by the self‐assembly encapsulation of recombinant ferritin gf1 from oyster ( crassostrea gigas)
publisher Wiley
publishDate 2024
url http://dx.doi.org/10.1002/jsfa.13163
https://onlinelibrary.wiley.com/doi/pdf/10.1002/jsfa.13163
genre Crassostrea gigas
genre_facet Crassostrea gigas
op_source Journal of the Science of Food and Agriculture
volume 104, issue 5, page 2783-2791
ISSN 0022-5142 1097-0010
op_rights http://onlinelibrary.wiley.com/termsAndConditions#vor
op_doi https://doi.org/10.1002/jsfa.13163
container_title Journal of the Science of Food and Agriculture
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