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Complexation of β‐lactoglobulin with gum arabic: Effect of heat treatment and enhanced encapsulation efficiency
Heat treatment is widely used in food industry. Proteins and polysaccharides as important natural polymers in food, under heat treatment, the interactions between them could mediate the conformation and functional properties of proteins. Thermally induced β‐lactoglobulin‐gum arabic complexes (β‐Lg‐G...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7958567/ https://www.ncbi.nlm.nih.gov/pubmed/33747454 http://dx.doi.org/10.1002/fsn3.2103 |
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author | Cao, Mengna Gao, Jian Li, Yang Liu, Chengzhi Shi, Jieyu Ni, Fangfang Ren, Gerui Xie, Hujun |
author_facet | Cao, Mengna Gao, Jian Li, Yang Liu, Chengzhi Shi, Jieyu Ni, Fangfang Ren, Gerui Xie, Hujun |
author_sort | Cao, Mengna |
collection | PubMed |
description | Heat treatment is widely used in food industry. Proteins and polysaccharides as important natural polymers in food, under heat treatment, the interactions between them could mediate the conformation and functional properties of proteins. Thermally induced β‐lactoglobulin‐gum arabic complexes (β‐Lg‐GA) were fabricated, and the effect of heat treatment on physicochemical properties of the complexes was systematically investigated. The average particle size of β‐Lg‐GA complexes decreased with temperature increased, at 85°C, a smaller size of 273 nm was obtained. A saturated adsorption of GA was found when mass ratio of β‐Lg/GA was <1:2. At pH = 4.2–7.0, electrostatic attraction between β‐Lg and GA was low and a fairly constant turbidity was observed, the formed composite particles had good stability to the pH value. Through UV, fluorescence, and FTIR spectroscopy, it was found that formation of the nanoparticles relied on thermal denaturation and aggregation of protein, the electrostatic, hydrophobic, and hydrogen bonding interactions between β‐Lg and GA were also important. Scanning electron microscope further indicated β‐Lg and GA had good compatibility, and the complexes had a spherical core–shell structure at molecular level. In addition, these prepared natural nanoparticles by heat treatment show significantly higher encapsulation efficiency for (‐)‐epigallocatechin‐3‐gallate (EGCG) than that of unheated, thus could be used as a promising carrier for biologically active substances. |
format | Online Article Text |
id | pubmed-7958567 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-79585672021-03-19 Complexation of β‐lactoglobulin with gum arabic: Effect of heat treatment and enhanced encapsulation efficiency Cao, Mengna Gao, Jian Li, Yang Liu, Chengzhi Shi, Jieyu Ni, Fangfang Ren, Gerui Xie, Hujun Food Sci Nutr Original Research Heat treatment is widely used in food industry. Proteins and polysaccharides as important natural polymers in food, under heat treatment, the interactions between them could mediate the conformation and functional properties of proteins. Thermally induced β‐lactoglobulin‐gum arabic complexes (β‐Lg‐GA) were fabricated, and the effect of heat treatment on physicochemical properties of the complexes was systematically investigated. The average particle size of β‐Lg‐GA complexes decreased with temperature increased, at 85°C, a smaller size of 273 nm was obtained. A saturated adsorption of GA was found when mass ratio of β‐Lg/GA was <1:2. At pH = 4.2–7.0, electrostatic attraction between β‐Lg and GA was low and a fairly constant turbidity was observed, the formed composite particles had good stability to the pH value. Through UV, fluorescence, and FTIR spectroscopy, it was found that formation of the nanoparticles relied on thermal denaturation and aggregation of protein, the electrostatic, hydrophobic, and hydrogen bonding interactions between β‐Lg and GA were also important. Scanning electron microscope further indicated β‐Lg and GA had good compatibility, and the complexes had a spherical core–shell structure at molecular level. In addition, these prepared natural nanoparticles by heat treatment show significantly higher encapsulation efficiency for (‐)‐epigallocatechin‐3‐gallate (EGCG) than that of unheated, thus could be used as a promising carrier for biologically active substances. John Wiley and Sons Inc. 2021-01-18 /pmc/articles/PMC7958567/ /pubmed/33747454 http://dx.doi.org/10.1002/fsn3.2103 Text en © 2021 The Authors. Food Science & Nutrition published by Wiley Periodicals LLC This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Research Cao, Mengna Gao, Jian Li, Yang Liu, Chengzhi Shi, Jieyu Ni, Fangfang Ren, Gerui Xie, Hujun Complexation of β‐lactoglobulin with gum arabic: Effect of heat treatment and enhanced encapsulation efficiency |
title | Complexation of β‐lactoglobulin with gum arabic: Effect of heat treatment and enhanced encapsulation efficiency |
title_full | Complexation of β‐lactoglobulin with gum arabic: Effect of heat treatment and enhanced encapsulation efficiency |
title_fullStr | Complexation of β‐lactoglobulin with gum arabic: Effect of heat treatment and enhanced encapsulation efficiency |
title_full_unstemmed | Complexation of β‐lactoglobulin with gum arabic: Effect of heat treatment and enhanced encapsulation efficiency |
title_short | Complexation of β‐lactoglobulin with gum arabic: Effect of heat treatment and enhanced encapsulation efficiency |
title_sort | complexation of β‐lactoglobulin with gum arabic: effect of heat treatment and enhanced encapsulation efficiency |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7958567/ https://www.ncbi.nlm.nih.gov/pubmed/33747454 http://dx.doi.org/10.1002/fsn3.2103 |
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