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Interfacial characteristics, colloidal properties and storage stability of dairy protein-stabilized emulsion as a function of heating and homogenization

This research investigated the influence of processing history on physicochemical properties of dairy protein-stabilized emulsions. Emulsions were heated (UHT) either before or after a single homogenization (UHTSH, SHUHT) or homogenized both before and after heating (double homogenization, DHUHT). T...

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Autores principales: Li, Quanyang, Zhao, Zhengtao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9050489/
https://www.ncbi.nlm.nih.gov/pubmed/35496589
http://dx.doi.org/10.1039/d0ra00677g
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author Li, Quanyang
Zhao, Zhengtao
author_facet Li, Quanyang
Zhao, Zhengtao
author_sort Li, Quanyang
collection PubMed
description This research investigated the influence of processing history on physicochemical properties of dairy protein-stabilized emulsions. Emulsions were heated (UHT) either before or after a single homogenization (UHTSH, SHUHT) or homogenized both before and after heating (double homogenization, DHUHT). The results demonstrated that UHT treatment increased the protein load at the oil/water interface while homogenization prior to UHT (SHUHT) inhibited displacement of protein by surfactant molecules, and this emulsion exhibited higher interfacial protein coverage and wider size distribution compared to the emulsion produced by UHTSH. The use of the double homogenization with UHT resulted in emulsion droplets with the smallest average size and lowest concentration of unabsorbed protein. However, no difference in the protein load in a specific area was noticed between emulsions produced by DHUHT and SHUHT. When changes of surface tension at the air/water interface were measured using a drop tensiometer, SHUHT emulsion showed the fastest decrease of surface tension due to the occurrence of a lower level of surfactant displacement where more surfactant was available for fast adsorption. Emulsions prepared with DHUHT or UHTSH decreased the surface tension in a slower speed than SHUHT. During storage, partial coalescence of emulsion droplets was observed for emulsions produced with single homogenization, regardless of whether this was carried out before or after heating. Double homogenization formed more stable emulsions than single homogenization. This work clearly showed that it is possible to tailor physico-chemical functionalities of dairy protein-based emulsions by controlling the interactions between proteins or with surfactants during processing.
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spelling pubmed-90504892022-04-29 Interfacial characteristics, colloidal properties and storage stability of dairy protein-stabilized emulsion as a function of heating and homogenization Li, Quanyang Zhao, Zhengtao RSC Adv Chemistry This research investigated the influence of processing history on physicochemical properties of dairy protein-stabilized emulsions. Emulsions were heated (UHT) either before or after a single homogenization (UHTSH, SHUHT) or homogenized both before and after heating (double homogenization, DHUHT). The results demonstrated that UHT treatment increased the protein load at the oil/water interface while homogenization prior to UHT (SHUHT) inhibited displacement of protein by surfactant molecules, and this emulsion exhibited higher interfacial protein coverage and wider size distribution compared to the emulsion produced by UHTSH. The use of the double homogenization with UHT resulted in emulsion droplets with the smallest average size and lowest concentration of unabsorbed protein. However, no difference in the protein load in a specific area was noticed between emulsions produced by DHUHT and SHUHT. When changes of surface tension at the air/water interface were measured using a drop tensiometer, SHUHT emulsion showed the fastest decrease of surface tension due to the occurrence of a lower level of surfactant displacement where more surfactant was available for fast adsorption. Emulsions prepared with DHUHT or UHTSH decreased the surface tension in a slower speed than SHUHT. During storage, partial coalescence of emulsion droplets was observed for emulsions produced with single homogenization, regardless of whether this was carried out before or after heating. Double homogenization formed more stable emulsions than single homogenization. This work clearly showed that it is possible to tailor physico-chemical functionalities of dairy protein-based emulsions by controlling the interactions between proteins or with surfactants during processing. The Royal Society of Chemistry 2020-03-25 /pmc/articles/PMC9050489/ /pubmed/35496589 http://dx.doi.org/10.1039/d0ra00677g Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/
spellingShingle Chemistry
Li, Quanyang
Zhao, Zhengtao
Interfacial characteristics, colloidal properties and storage stability of dairy protein-stabilized emulsion as a function of heating and homogenization
title Interfacial characteristics, colloidal properties and storage stability of dairy protein-stabilized emulsion as a function of heating and homogenization
title_full Interfacial characteristics, colloidal properties and storage stability of dairy protein-stabilized emulsion as a function of heating and homogenization
title_fullStr Interfacial characteristics, colloidal properties and storage stability of dairy protein-stabilized emulsion as a function of heating and homogenization
title_full_unstemmed Interfacial characteristics, colloidal properties and storage stability of dairy protein-stabilized emulsion as a function of heating and homogenization
title_short Interfacial characteristics, colloidal properties and storage stability of dairy protein-stabilized emulsion as a function of heating and homogenization
title_sort interfacial characteristics, colloidal properties and storage stability of dairy protein-stabilized emulsion as a function of heating and homogenization
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9050489/
https://www.ncbi.nlm.nih.gov/pubmed/35496589
http://dx.doi.org/10.1039/d0ra00677g
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AT zhaozhengtao interfacialcharacteristicscolloidalpropertiesandstoragestabilityofdairyproteinstabilizedemulsionasafunctionofheatingandhomogenization