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A novel strategy for improving the stability of myofibrillar protein emulsions at low ionic strength using high-intensity ultrasound combined with non-enzymatic glycation
Poor emulsification of myofibrillar proteins (MPs) limits the production of meat protein emulsion-type products, and it is related to the myosin self-assembles in low-salt settings. The effect of high-intensity ultrasound (HIU) pretreatment combined with non-enzymatic glycation on MP-stabilized emul...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10692711/ https://www.ncbi.nlm.nih.gov/pubmed/37979277 http://dx.doi.org/10.1016/j.ultsonch.2023.106694 |
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author | Han, Ge Zhao, Siqi Sun, Fangda Xia, Xiufang Liu, Haotian Kong, Baohua |
author_facet | Han, Ge Zhao, Siqi Sun, Fangda Xia, Xiufang Liu, Haotian Kong, Baohua |
author_sort | Han, Ge |
collection | PubMed |
description | Poor emulsification of myofibrillar proteins (MPs) limits the production of meat protein emulsion-type products, and it is related to the myosin self-assembles in low-salt settings. The effect of high-intensity ultrasound (HIU) pretreatment combined with non-enzymatic glycation on MP-stabilized emulsions in low-salt settings was investigated in this study, and the potential mechanism was revealed. The results indicated that, compared to using either HIU or glycation treatment alone, HIU pretreatment in combination with glycation significantly improves the physical stability of emulsions while increasing the distribution uniformity and reducing the droplet particle size from 18.05 μm to 2.54 μm (P < 0.05). Correspondingly, the emulsion prepared using this approach exhibited a relatively high absolute zeta potential (−23.58 mV) and a high interfacial protein content (38.78 %) (P < 0.05), promoting molecular rearrangement and forming a continuous and stable interfacial layer. HIU pretreatment combined with glycation could offer reinforced electrostatic repulsion and steric hindrance to depolymerize self-assembled filamentous polymers, thus enhancing the stability of droplets. Additionally, the thermal sensitivity of the glycated MPs pretreated by HIU was remarkably reduced, thus improving the thermal stability of the corresponding emulsions. |
format | Online Article Text |
id | pubmed-10692711 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-106927112023-12-03 A novel strategy for improving the stability of myofibrillar protein emulsions at low ionic strength using high-intensity ultrasound combined with non-enzymatic glycation Han, Ge Zhao, Siqi Sun, Fangda Xia, Xiufang Liu, Haotian Kong, Baohua Ultrason Sonochem Original Research Article Poor emulsification of myofibrillar proteins (MPs) limits the production of meat protein emulsion-type products, and it is related to the myosin self-assembles in low-salt settings. The effect of high-intensity ultrasound (HIU) pretreatment combined with non-enzymatic glycation on MP-stabilized emulsions in low-salt settings was investigated in this study, and the potential mechanism was revealed. The results indicated that, compared to using either HIU or glycation treatment alone, HIU pretreatment in combination with glycation significantly improves the physical stability of emulsions while increasing the distribution uniformity and reducing the droplet particle size from 18.05 μm to 2.54 μm (P < 0.05). Correspondingly, the emulsion prepared using this approach exhibited a relatively high absolute zeta potential (−23.58 mV) and a high interfacial protein content (38.78 %) (P < 0.05), promoting molecular rearrangement and forming a continuous and stable interfacial layer. HIU pretreatment combined with glycation could offer reinforced electrostatic repulsion and steric hindrance to depolymerize self-assembled filamentous polymers, thus enhancing the stability of droplets. Additionally, the thermal sensitivity of the glycated MPs pretreated by HIU was remarkably reduced, thus improving the thermal stability of the corresponding emulsions. Elsevier 2023-11-15 /pmc/articles/PMC10692711/ /pubmed/37979277 http://dx.doi.org/10.1016/j.ultsonch.2023.106694 Text en © 2023 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Original Research Article Han, Ge Zhao, Siqi Sun, Fangda Xia, Xiufang Liu, Haotian Kong, Baohua A novel strategy for improving the stability of myofibrillar protein emulsions at low ionic strength using high-intensity ultrasound combined with non-enzymatic glycation |
title | A novel strategy for improving the stability of myofibrillar protein emulsions at low ionic strength using high-intensity ultrasound combined with non-enzymatic glycation |
title_full | A novel strategy for improving the stability of myofibrillar protein emulsions at low ionic strength using high-intensity ultrasound combined with non-enzymatic glycation |
title_fullStr | A novel strategy for improving the stability of myofibrillar protein emulsions at low ionic strength using high-intensity ultrasound combined with non-enzymatic glycation |
title_full_unstemmed | A novel strategy for improving the stability of myofibrillar protein emulsions at low ionic strength using high-intensity ultrasound combined with non-enzymatic glycation |
title_short | A novel strategy for improving the stability of myofibrillar protein emulsions at low ionic strength using high-intensity ultrasound combined with non-enzymatic glycation |
title_sort | novel strategy for improving the stability of myofibrillar protein emulsions at low ionic strength using high-intensity ultrasound combined with non-enzymatic glycation |
topic | Original Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10692711/ https://www.ncbi.nlm.nih.gov/pubmed/37979277 http://dx.doi.org/10.1016/j.ultsonch.2023.106694 |
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