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Formation and Characterization of β-Lactoglobulin and Gum Arabic Complexes: The Role of pH
Protein–polysaccharide complexes have received increasing attention as delivery systems to improve the stability and bioavailability of multiple bioactive compounds. However, deep and comprehensive understanding of the interactions between proteins and polysaccharides is still required for enhancing...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7504125/ https://www.ncbi.nlm.nih.gov/pubmed/32854454 http://dx.doi.org/10.3390/molecules25173871 |
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author | Wang, Ziyuan Liu, Jie Gao, Jian Cao, Mengna Ren, Gerui Xie, Hunjun Yao, Mingfei |
author_facet | Wang, Ziyuan Liu, Jie Gao, Jian Cao, Mengna Ren, Gerui Xie, Hunjun Yao, Mingfei |
author_sort | Wang, Ziyuan |
collection | PubMed |
description | Protein–polysaccharide complexes have received increasing attention as delivery systems to improve the stability and bioavailability of multiple bioactive compounds. However, deep and comprehensive understanding of the interactions between proteins and polysaccharides is still required for enhancing their loading efficiency and facilitating targeted delivery. In this study, we fabricated a type of protein–polysaccharide complexes using food-grade materials of β-lactoglobulin (β-Lg) and gum arabic (GA). The formation and characteristics of β-Lg–GA complexes were investigated by determining the influence of pH and other factors on their turbidity, zeta-potential, particle size and rheology. Results demonstrated that the β-Lg and GA suspension experienced four regimes including co-soluble polymers, soluble complexes, insoluble complexes and co-soluble polymers when the pH ranged from 1.2 to 7 and that β-Lg–GA complexes formed in large quantities at pH 4.2. An increased ratio of β-Lg in the mixtures was found to promote the formation of β-Lg and GA complexes, and the optimal β-Lg/GA ratio was found to be 2:1. The electrostatic interactions between the NH(3)(+) group in β-Lg and the COO(−) group in GA were confirmed to be the main driving forces for the formation of β-Lg/GA complexes. The formed structure also resulted in enhanced thermal stability and viscosity. These findings provide critical implications for the application of β-lactoglobulin and gum arabic complexes in food research and industry. |
format | Online Article Text |
id | pubmed-7504125 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-75041252020-09-24 Formation and Characterization of β-Lactoglobulin and Gum Arabic Complexes: The Role of pH Wang, Ziyuan Liu, Jie Gao, Jian Cao, Mengna Ren, Gerui Xie, Hunjun Yao, Mingfei Molecules Article Protein–polysaccharide complexes have received increasing attention as delivery systems to improve the stability and bioavailability of multiple bioactive compounds. However, deep and comprehensive understanding of the interactions between proteins and polysaccharides is still required for enhancing their loading efficiency and facilitating targeted delivery. In this study, we fabricated a type of protein–polysaccharide complexes using food-grade materials of β-lactoglobulin (β-Lg) and gum arabic (GA). The formation and characteristics of β-Lg–GA complexes were investigated by determining the influence of pH and other factors on their turbidity, zeta-potential, particle size and rheology. Results demonstrated that the β-Lg and GA suspension experienced four regimes including co-soluble polymers, soluble complexes, insoluble complexes and co-soluble polymers when the pH ranged from 1.2 to 7 and that β-Lg–GA complexes formed in large quantities at pH 4.2. An increased ratio of β-Lg in the mixtures was found to promote the formation of β-Lg and GA complexes, and the optimal β-Lg/GA ratio was found to be 2:1. The electrostatic interactions between the NH(3)(+) group in β-Lg and the COO(−) group in GA were confirmed to be the main driving forces for the formation of β-Lg/GA complexes. The formed structure also resulted in enhanced thermal stability and viscosity. These findings provide critical implications for the application of β-lactoglobulin and gum arabic complexes in food research and industry. MDPI 2020-08-25 /pmc/articles/PMC7504125/ /pubmed/32854454 http://dx.doi.org/10.3390/molecules25173871 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Wang, Ziyuan Liu, Jie Gao, Jian Cao, Mengna Ren, Gerui Xie, Hunjun Yao, Mingfei Formation and Characterization of β-Lactoglobulin and Gum Arabic Complexes: The Role of pH |
title | Formation and Characterization of β-Lactoglobulin and Gum Arabic Complexes: The Role of pH |
title_full | Formation and Characterization of β-Lactoglobulin and Gum Arabic Complexes: The Role of pH |
title_fullStr | Formation and Characterization of β-Lactoglobulin and Gum Arabic Complexes: The Role of pH |
title_full_unstemmed | Formation and Characterization of β-Lactoglobulin and Gum Arabic Complexes: The Role of pH |
title_short | Formation and Characterization of β-Lactoglobulin and Gum Arabic Complexes: The Role of pH |
title_sort | formation and characterization of β-lactoglobulin and gum arabic complexes: the role of ph |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7504125/ https://www.ncbi.nlm.nih.gov/pubmed/32854454 http://dx.doi.org/10.3390/molecules25173871 |
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