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Formation mechanism of binary complex based on β-lactoglobulin and propylene glycol alginate with different molecular weights: Structural characterization and delivery of curcumin
The complexation of protein and polysaccharide has shown considerable potential for the encapsulation of functional food components. In this work, propylene glycol alginate (PGA) molecules with different molecular weights (100, 500, and 2,000 kDa) were prepared through H(2)O(2) oxidation, which were...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9344013/ https://www.ncbi.nlm.nih.gov/pubmed/35928836 http://dx.doi.org/10.3389/fnut.2022.965600 |
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author | Lin, Dongdong Su, Jiaqi Chen, Shuai Wei, Jiao Zhang, Liang Li, Xiude Yuan, Fang |
author_facet | Lin, Dongdong Su, Jiaqi Chen, Shuai Wei, Jiao Zhang, Liang Li, Xiude Yuan, Fang |
author_sort | Lin, Dongdong |
collection | PubMed |
description | The complexation of protein and polysaccharide has shown considerable potential for the encapsulation of functional food components. In this work, propylene glycol alginate (PGA) molecules with different molecular weights (100, 500, and 2,000 kDa) were prepared through H(2)O(2) oxidation, which were further combined with β-lactoglobulin nanoparticles (β-lgNPs) to form PGA-β-lgNPs complexes for the delivery of curcumin (Cur). Results showed that the depolymerization of PGA molecule was resulted from the breakage of glycosidic bonds in the main chain, and the depolymerization rate of PGA molecule depended on the reaction time, temperature, solution pH and H(2)O(2) concentration. As the increasing molecular weight of PGA, the particle size, zeta-potential and turbidity of the complexes were obviously increased. The formation of PGA/β-lgNPs complexes was mainly driven by non-covalent interaction, including electrostatic gravitational interaction, hydrogen bonding and hydrophobic effect. Interestingly, the difference in the molecular weight of PGA also led to significantly differences in the micro-morphology of the complexes, as PGA with a high molecular weight (2,000 kDa) generated the formation of a “fruit-tree” shaped structure, whereas PGA with relatively low molecular weight (100 and 500 kDa) led to spherical particles with a “core-shell” structure. In addition, the incorporation of PGA molecules into β-lgNPs dispersion also contributed to the improvement in the encapsulation efficiency of Cur as well as physicochemical stability of β-lgNPs, and PGA with a higher molecular weight was confirmed with a better effect. Findings in the current work may help to further understand the effect of molecular weight of polysaccharide on the physical and structural properties as well as effectiveness as delivery systems of polysaccharide-protein complexes, providing for the possibility for the design and development of more efficient carriers for bioactive compounds in food system. |
format | Online Article Text |
id | pubmed-9344013 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-93440132022-08-03 Formation mechanism of binary complex based on β-lactoglobulin and propylene glycol alginate with different molecular weights: Structural characterization and delivery of curcumin Lin, Dongdong Su, Jiaqi Chen, Shuai Wei, Jiao Zhang, Liang Li, Xiude Yuan, Fang Front Nutr Nutrition The complexation of protein and polysaccharide has shown considerable potential for the encapsulation of functional food components. In this work, propylene glycol alginate (PGA) molecules with different molecular weights (100, 500, and 2,000 kDa) were prepared through H(2)O(2) oxidation, which were further combined with β-lactoglobulin nanoparticles (β-lgNPs) to form PGA-β-lgNPs complexes for the delivery of curcumin (Cur). Results showed that the depolymerization of PGA molecule was resulted from the breakage of glycosidic bonds in the main chain, and the depolymerization rate of PGA molecule depended on the reaction time, temperature, solution pH and H(2)O(2) concentration. As the increasing molecular weight of PGA, the particle size, zeta-potential and turbidity of the complexes were obviously increased. The formation of PGA/β-lgNPs complexes was mainly driven by non-covalent interaction, including electrostatic gravitational interaction, hydrogen bonding and hydrophobic effect. Interestingly, the difference in the molecular weight of PGA also led to significantly differences in the micro-morphology of the complexes, as PGA with a high molecular weight (2,000 kDa) generated the formation of a “fruit-tree” shaped structure, whereas PGA with relatively low molecular weight (100 and 500 kDa) led to spherical particles with a “core-shell” structure. In addition, the incorporation of PGA molecules into β-lgNPs dispersion also contributed to the improvement in the encapsulation efficiency of Cur as well as physicochemical stability of β-lgNPs, and PGA with a higher molecular weight was confirmed with a better effect. Findings in the current work may help to further understand the effect of molecular weight of polysaccharide on the physical and structural properties as well as effectiveness as delivery systems of polysaccharide-protein complexes, providing for the possibility for the design and development of more efficient carriers for bioactive compounds in food system. Frontiers Media S.A. 2022-07-19 /pmc/articles/PMC9344013/ /pubmed/35928836 http://dx.doi.org/10.3389/fnut.2022.965600 Text en Copyright © 2022 Lin, Su, Chen, Wei, Zhang, Li and Yuan. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Nutrition Lin, Dongdong Su, Jiaqi Chen, Shuai Wei, Jiao Zhang, Liang Li, Xiude Yuan, Fang Formation mechanism of binary complex based on β-lactoglobulin and propylene glycol alginate with different molecular weights: Structural characterization and delivery of curcumin |
title | Formation mechanism of binary complex based on β-lactoglobulin and propylene glycol alginate with different molecular weights: Structural characterization and delivery of curcumin |
title_full | Formation mechanism of binary complex based on β-lactoglobulin and propylene glycol alginate with different molecular weights: Structural characterization and delivery of curcumin |
title_fullStr | Formation mechanism of binary complex based on β-lactoglobulin and propylene glycol alginate with different molecular weights: Structural characterization and delivery of curcumin |
title_full_unstemmed | Formation mechanism of binary complex based on β-lactoglobulin and propylene glycol alginate with different molecular weights: Structural characterization and delivery of curcumin |
title_short | Formation mechanism of binary complex based on β-lactoglobulin and propylene glycol alginate with different molecular weights: Structural characterization and delivery of curcumin |
title_sort | formation mechanism of binary complex based on β-lactoglobulin and propylene glycol alginate with different molecular weights: structural characterization and delivery of curcumin |
topic | Nutrition |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9344013/ https://www.ncbi.nlm.nih.gov/pubmed/35928836 http://dx.doi.org/10.3389/fnut.2022.965600 |
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