Effect of heat, pH, ultrasonication and ethanol on the denaturation of whey protein isolate using a newly developed approach in the analysis of difference-UV spectra.
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| Title: | Effect of heat, pH, ultrasonication and ethanol on the denaturation of whey protein isolate using a newly developed approach in the analysis of difference-UV spectra. |
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| Authors: | Nikolaidis, Athanasios1, Andreadis, Marios1, Moschakis, Thomas1 tmoschak@agro.auth.gr |
| Source: | Food Chemistry. Oct2017, Vol. 232, p425-433. 9p. |
| Subjects: | Ethanol, Denaturation of proteins, Whey proteins, Sonication, Heat stability in proteins |
| Abstract: | A newly developed method of analysis of difference-UV spectra was successfully implemented in the study of the effect of heat, pH, ultrasonication and ethanol on the denaturation of whey protein isolate. It was found that whey proteins exhibit their highest stability against heat denaturation at pH 3.75. At very low pH values, i.e. 2.5, they exhibited considerable cold denaturation, while after heating at this pH value, the supplementary heat denaturation rate was lower compared to that at neutral pH. The highest heat denaturation rates were observed at pH values higher than neutral. High power sonication on whey proteins, previously heated at 90 °C for 30 min, resulted in a rather small reduction of the fraction of the heat denatured protein aggregates. Finally, when ethanol was used as a cosolvent in the concentration range 20–50%, a sharp increase in the degree of denaturation, compared to the native protein solution, was observed. [ABSTRACT FROM AUTHOR] |
| Copyright of Food Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 122911520 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Effect of heat, pH, ultrasonication and ethanol on the denaturation of whey protein isolate using a newly developed approach in the analysis of difference-UV spectra. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Nikolaidis%2C+Athanasios%22">Nikolaidis, Athanasios</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Andreadis%2C+Marios%22">Andreadis, Marios</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Moschakis%2C+Thomas%22">Moschakis, Thomas</searchLink><relatesTo>1</relatesTo><i> tmoschak@agro.auth.gr</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Food+Chemistry%22">Food Chemistry</searchLink>. Oct2017, Vol. 232, p425-433. 9p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Ethanol%22">Ethanol</searchLink><br /><searchLink fieldCode="DE" term="%22Denaturation+of+proteins%22">Denaturation of proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Whey+proteins%22">Whey proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Sonication%22">Sonication</searchLink><br /><searchLink fieldCode="DE" term="%22Heat+stability+in+proteins%22">Heat stability in proteins</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: A newly developed method of analysis of difference-UV spectra was successfully implemented in the study of the effect of heat, pH, ultrasonication and ethanol on the denaturation of whey protein isolate. It was found that whey proteins exhibit their highest stability against heat denaturation at pH 3.75. At very low pH values, i.e. 2.5, they exhibited considerable cold denaturation, while after heating at this pH value, the supplementary heat denaturation rate was lower compared to that at neutral pH. The highest heat denaturation rates were observed at pH values higher than neutral. High power sonication on whey proteins, previously heated at 90 °C for 30 min, resulted in a rather small reduction of the fraction of the heat denatured protein aggregates. Finally, when ethanol was used as a cosolvent in the concentration range 20–50%, a sharp increase in the degree of denaturation, compared to the native protein solution, was observed. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Food Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.foodchem.2017.04.022 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 9 StartPage: 425 Subjects: – SubjectFull: Ethanol Type: general – SubjectFull: Denaturation of proteins Type: general – SubjectFull: Whey proteins Type: general – SubjectFull: Sonication Type: general – SubjectFull: Heat stability in proteins Type: general Titles: – TitleFull: Effect of heat, pH, ultrasonication and ethanol on the denaturation of whey protein isolate using a newly developed approach in the analysis of difference-UV spectra. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Nikolaidis, Athanasios – PersonEntity: Name: NameFull: Andreadis, Marios – PersonEntity: Name: NameFull: Moschakis, Thomas IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 10 Text: Oct2017 Type: published Y: 2017 Identifiers: – Type: issn-print Value: 03088146 Numbering: – Type: volume Value: 232 Titles: – TitleFull: Food Chemistry Type: main |
| ResultId | 1 |
