Characterization of coacervation behavior between whey protein isolate and propylene glycol alginate: A morphology, spectroscopy, and thermodynamics study

The interactions between whey protein isolate (WPI) and propylene glycol alginate (PGA) were investigated as a function of pH and the mass ratio. The results showed that WPI and PGA formed a soluble and uniform complex at a mass ratio of 2:1 and pH 4.0 through forces such as electrostatic attraction...

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Autores principales: Xi, Chunyu, Sun, Zhengwei, Chen, Xing, Ding, Xuan, Zhang, Tiehua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9532732/
https://www.ncbi.nlm.nih.gov/pubmed/36211725
http://dx.doi.org/10.1016/j.fochx.2022.100402
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author Xi, Chunyu
Sun, Zhengwei
Chen, Xing
Ding, Xuan
Zhang, Tiehua
author_facet Xi, Chunyu
Sun, Zhengwei
Chen, Xing
Ding, Xuan
Zhang, Tiehua
author_sort Xi, Chunyu
collection PubMed
description The interactions between whey protein isolate (WPI) and propylene glycol alginate (PGA) were investigated as a function of pH and the mass ratio. The results showed that WPI and PGA formed a soluble and uniform complex at a mass ratio of 2:1 and pH 4.0 through forces such as electrostatic attraction and hydrogen bonding. Isothermal titration calorimetry confirmed that the contribution of positive enthalpy (ΔH) and entropy (ΔS) were the beneficial indicator in the process of combining WPI and PGA under the same mass ratio but different pH. Fourier transform infrared spectroscopy, fluorescence spectroscopy and circular dichroism confirmed that hydrogen bonding was also one of the interaction forces in addition to electrostatic interactions between WPI-PGA complex. The freeze-dried WPI-PGA complex showed the same amorphous structure as WPI. These formed WPI-PGA complexes provided insights for interaction mechanism of proteins and polysaccharides as well as a theoretical basis for the food industry.
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spelling pubmed-95327322022-10-06 Characterization of coacervation behavior between whey protein isolate and propylene glycol alginate: A morphology, spectroscopy, and thermodynamics study Xi, Chunyu Sun, Zhengwei Chen, Xing Ding, Xuan Zhang, Tiehua Food Chem X Research Article The interactions between whey protein isolate (WPI) and propylene glycol alginate (PGA) were investigated as a function of pH and the mass ratio. The results showed that WPI and PGA formed a soluble and uniform complex at a mass ratio of 2:1 and pH 4.0 through forces such as electrostatic attraction and hydrogen bonding. Isothermal titration calorimetry confirmed that the contribution of positive enthalpy (ΔH) and entropy (ΔS) were the beneficial indicator in the process of combining WPI and PGA under the same mass ratio but different pH. Fourier transform infrared spectroscopy, fluorescence spectroscopy and circular dichroism confirmed that hydrogen bonding was also one of the interaction forces in addition to electrostatic interactions between WPI-PGA complex. The freeze-dried WPI-PGA complex showed the same amorphous structure as WPI. These formed WPI-PGA complexes provided insights for interaction mechanism of proteins and polysaccharides as well as a theoretical basis for the food industry. Elsevier 2022-07-26 /pmc/articles/PMC9532732/ /pubmed/36211725 http://dx.doi.org/10.1016/j.fochx.2022.100402 Text en © 2022 The Authors 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 Research Article
Xi, Chunyu
Sun, Zhengwei
Chen, Xing
Ding, Xuan
Zhang, Tiehua
Characterization of coacervation behavior between whey protein isolate and propylene glycol alginate: A morphology, spectroscopy, and thermodynamics study
title Characterization of coacervation behavior between whey protein isolate and propylene glycol alginate: A morphology, spectroscopy, and thermodynamics study
title_full Characterization of coacervation behavior between whey protein isolate and propylene glycol alginate: A morphology, spectroscopy, and thermodynamics study
title_fullStr Characterization of coacervation behavior between whey protein isolate and propylene glycol alginate: A morphology, spectroscopy, and thermodynamics study
title_full_unstemmed Characterization of coacervation behavior between whey protein isolate and propylene glycol alginate: A morphology, spectroscopy, and thermodynamics study
title_short Characterization of coacervation behavior between whey protein isolate and propylene glycol alginate: A morphology, spectroscopy, and thermodynamics study
title_sort characterization of coacervation behavior between whey protein isolate and propylene glycol alginate: a morphology, spectroscopy, and thermodynamics study
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9532732/
https://www.ncbi.nlm.nih.gov/pubmed/36211725
http://dx.doi.org/10.1016/j.fochx.2022.100402
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