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Oxidation of whey protein isolate after thermal convection and microwave heating and freeze-drying: Correlation among physicochemical and NIR spectroscopy analyses

This study investigated the oxidative susceptibility of whey protein isolate (WPI) dispersions treated by microwave or thermal convection before freeze-drying. WPI (20 mg protein/mL) in distilled water (DW) was heated at 63 ± 2 °C for 30 min by microwave (WPI-MW) or convection heating (WPI–CH) and f...

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Autores principales: Bordignon, Juliany Cristiny Sonda, Badaró, Amanda Teixeira, Barbin, Douglas Fernandes, Mariutti, Lilian Regina Barros, Netto, Flavia Maria
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10373659/
https://www.ncbi.nlm.nih.gov/pubmed/37519701
http://dx.doi.org/10.1016/j.heliyon.2023.e17981
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author Bordignon, Juliany Cristiny Sonda
Badaró, Amanda Teixeira
Barbin, Douglas Fernandes
Mariutti, Lilian Regina Barros
Netto, Flavia Maria
author_facet Bordignon, Juliany Cristiny Sonda
Badaró, Amanda Teixeira
Barbin, Douglas Fernandes
Mariutti, Lilian Regina Barros
Netto, Flavia Maria
author_sort Bordignon, Juliany Cristiny Sonda
collection PubMed
description This study investigated the oxidative susceptibility of whey protein isolate (WPI) dispersions treated by microwave or thermal convection before freeze-drying. WPI (20 mg protein/mL) in distilled water (DW) was heated at 63 ± 2 °C for 30 min by microwave (WPI-MW) or convection heating (WPI–CH) and freeze-dried. Untreated WPI (WPI–C), WPI solubilized in DW and freeze-dried (WPI-FD), and WPI solubilized in DW, heated at 98 ± 2 °C for 2 min and freeze-dried (WPI–B) were also evaluated. Structural changes (turbidity, ζ potential, SDS-PAGE, and near-infrared spectroscopy (NIR)) and protein oxidation (dityrosine, protein carbonylation, and SH groups) were investigated. WPI-FD showed alterations compared to WPI-C, mainly concerning carbonyl groups. Microwave heating increased carbonyl groups and dityrosine formation compared to conventional heating. NIR spectrum indicated changes related to the formation of carbonyl groups and PCA analysis allowed us to distinguish the samples according to carbonyl group content. The results suggest that NIR may contribute to monitoring oxidative changes in proteins resulting from processing.
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spelling pubmed-103736592023-07-28 Oxidation of whey protein isolate after thermal convection and microwave heating and freeze-drying: Correlation among physicochemical and NIR spectroscopy analyses Bordignon, Juliany Cristiny Sonda Badaró, Amanda Teixeira Barbin, Douglas Fernandes Mariutti, Lilian Regina Barros Netto, Flavia Maria Heliyon Research Article This study investigated the oxidative susceptibility of whey protein isolate (WPI) dispersions treated by microwave or thermal convection before freeze-drying. WPI (20 mg protein/mL) in distilled water (DW) was heated at 63 ± 2 °C for 30 min by microwave (WPI-MW) or convection heating (WPI–CH) and freeze-dried. Untreated WPI (WPI–C), WPI solubilized in DW and freeze-dried (WPI-FD), and WPI solubilized in DW, heated at 98 ± 2 °C for 2 min and freeze-dried (WPI–B) were also evaluated. Structural changes (turbidity, ζ potential, SDS-PAGE, and near-infrared spectroscopy (NIR)) and protein oxidation (dityrosine, protein carbonylation, and SH groups) were investigated. WPI-FD showed alterations compared to WPI-C, mainly concerning carbonyl groups. Microwave heating increased carbonyl groups and dityrosine formation compared to conventional heating. NIR spectrum indicated changes related to the formation of carbonyl groups and PCA analysis allowed us to distinguish the samples according to carbonyl group content. The results suggest that NIR may contribute to monitoring oxidative changes in proteins resulting from processing. Elsevier 2023-07-06 /pmc/articles/PMC10373659/ /pubmed/37519701 http://dx.doi.org/10.1016/j.heliyon.2023.e17981 Text en © 2023 Published by Elsevier Ltd. 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
Bordignon, Juliany Cristiny Sonda
Badaró, Amanda Teixeira
Barbin, Douglas Fernandes
Mariutti, Lilian Regina Barros
Netto, Flavia Maria
Oxidation of whey protein isolate after thermal convection and microwave heating and freeze-drying: Correlation among physicochemical and NIR spectroscopy analyses
title Oxidation of whey protein isolate after thermal convection and microwave heating and freeze-drying: Correlation among physicochemical and NIR spectroscopy analyses
title_full Oxidation of whey protein isolate after thermal convection and microwave heating and freeze-drying: Correlation among physicochemical and NIR spectroscopy analyses
title_fullStr Oxidation of whey protein isolate after thermal convection and microwave heating and freeze-drying: Correlation among physicochemical and NIR spectroscopy analyses
title_full_unstemmed Oxidation of whey protein isolate after thermal convection and microwave heating and freeze-drying: Correlation among physicochemical and NIR spectroscopy analyses
title_short Oxidation of whey protein isolate after thermal convection and microwave heating and freeze-drying: Correlation among physicochemical and NIR spectroscopy analyses
title_sort oxidation of whey protein isolate after thermal convection and microwave heating and freeze-drying: correlation among physicochemical and nir spectroscopy analyses
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10373659/
https://www.ncbi.nlm.nih.gov/pubmed/37519701
http://dx.doi.org/10.1016/j.heliyon.2023.e17981
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