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Structure and stability characterization of pea protein isolate-xylan conjugate-stabilized nanoemulsions prepared using ultrasound homogenization
Preparation of pea protein isolate-xylan (PPI-X) conjugate-stabilized nanoemulsions using ultrasonic homogenization and the corresponding structure and environmental stability were investigated in this study. Conditions used to prepare nanoemulsions were optimized using a response surface methodolog...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9576981/ https://www.ncbi.nlm.nih.gov/pubmed/36240589 http://dx.doi.org/10.1016/j.ultsonch.2022.106195 |
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author | Zhao, Dan Ge, Yuhong Xiang, Xianrong Dong, Hongmin Qin, Wen Zhang, Qing |
author_facet | Zhao, Dan Ge, Yuhong Xiang, Xianrong Dong, Hongmin Qin, Wen Zhang, Qing |
author_sort | Zhao, Dan |
collection | PubMed |
description | Preparation of pea protein isolate-xylan (PPI-X) conjugate-stabilized nanoemulsions using ultrasonic homogenization and the corresponding structure and environmental stability were investigated in this study. Conditions used to prepare nanoemulsions were optimized using a response surface methodology as follows: protein concentration 8.86 mg/mL, ultrasound amplitudes 57 % (370.5 W), and ultrasound time 16 min. PPI-X conjugate-stabilized nanoemulsions formed under these conditions exhibited less mean droplet size (189.4 ± 0.45 nm), more uniform droplet distribution, greater absolute value of zeta-potential (44.8 ± 0.22 mV), and higher protein adsorption content compared with PPI-stabilized nanoemulsions. PPI-X conjugate-stabilized nanoemulsions also exhibited even particle distribution and dense network structure, which might be reasons for the observed high interfacial protein adsorption content of conjugate-stabilized nanoemulsions. Moreover, better stability against environmental stresses, such as thermal treatment, freeze–thaw treatment, ionic strength and type, and storage time was also observed for the conjugate-stabilized nanoemulsions, indicating that this type of nanoemulsions possess a potential to endure harsh food processing conditions. Therefore, results provide a novel approach for the preparation of protein-polysaccharide conjugate-stabilized nanoemulsions to be applied as novel ingredients to meet special requirements of processed foods. |
format | Online Article Text |
id | pubmed-9576981 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-95769812022-10-19 Structure and stability characterization of pea protein isolate-xylan conjugate-stabilized nanoemulsions prepared using ultrasound homogenization Zhao, Dan Ge, Yuhong Xiang, Xianrong Dong, Hongmin Qin, Wen Zhang, Qing Ultrason Sonochem Short Communication Preparation of pea protein isolate-xylan (PPI-X) conjugate-stabilized nanoemulsions using ultrasonic homogenization and the corresponding structure and environmental stability were investigated in this study. Conditions used to prepare nanoemulsions were optimized using a response surface methodology as follows: protein concentration 8.86 mg/mL, ultrasound amplitudes 57 % (370.5 W), and ultrasound time 16 min. PPI-X conjugate-stabilized nanoemulsions formed under these conditions exhibited less mean droplet size (189.4 ± 0.45 nm), more uniform droplet distribution, greater absolute value of zeta-potential (44.8 ± 0.22 mV), and higher protein adsorption content compared with PPI-stabilized nanoemulsions. PPI-X conjugate-stabilized nanoemulsions also exhibited even particle distribution and dense network structure, which might be reasons for the observed high interfacial protein adsorption content of conjugate-stabilized nanoemulsions. Moreover, better stability against environmental stresses, such as thermal treatment, freeze–thaw treatment, ionic strength and type, and storage time was also observed for the conjugate-stabilized nanoemulsions, indicating that this type of nanoemulsions possess a potential to endure harsh food processing conditions. Therefore, results provide a novel approach for the preparation of protein-polysaccharide conjugate-stabilized nanoemulsions to be applied as novel ingredients to meet special requirements of processed foods. Elsevier 2022-10-10 /pmc/articles/PMC9576981/ /pubmed/36240589 http://dx.doi.org/10.1016/j.ultsonch.2022.106195 Text en © 2022 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 | Short Communication Zhao, Dan Ge, Yuhong Xiang, Xianrong Dong, Hongmin Qin, Wen Zhang, Qing Structure and stability characterization of pea protein isolate-xylan conjugate-stabilized nanoemulsions prepared using ultrasound homogenization |
title | Structure and stability characterization of pea protein isolate-xylan conjugate-stabilized nanoemulsions prepared using ultrasound homogenization |
title_full | Structure and stability characterization of pea protein isolate-xylan conjugate-stabilized nanoemulsions prepared using ultrasound homogenization |
title_fullStr | Structure and stability characterization of pea protein isolate-xylan conjugate-stabilized nanoemulsions prepared using ultrasound homogenization |
title_full_unstemmed | Structure and stability characterization of pea protein isolate-xylan conjugate-stabilized nanoemulsions prepared using ultrasound homogenization |
title_short | Structure and stability characterization of pea protein isolate-xylan conjugate-stabilized nanoemulsions prepared using ultrasound homogenization |
title_sort | structure and stability characterization of pea protein isolate-xylan conjugate-stabilized nanoemulsions prepared using ultrasound homogenization |
topic | Short Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9576981/ https://www.ncbi.nlm.nih.gov/pubmed/36240589 http://dx.doi.org/10.1016/j.ultsonch.2022.106195 |
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