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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...
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/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. |
format | Online Article Text |
id | pubmed-10373659 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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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