Increased stability and protease resistance of the β-lactoglobulin/vitamin D3 complex.
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| Title: | Increased stability and protease resistance of the β-lactoglobulin/vitamin D |
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| Authors: | Diarrassouba, Fatoumata1, Garrait, Ghislain2, Remondetto, Gabriel3, Alvarez, Pedro1, Beyssac, Eric2, Subirade, Muriel1 Muriel.Subirade@fsaa.ulaval.ca |
| Source: | Food Chemistry. Feb2014, Vol. 145, p646-652. 7p. |
| Subjects: | Proteolytic enzymes, Lactoglobulins, Vitamin D, Chemical stability, Complexation reactions, Bioavailability |
| Abstract: | Highlights: [•] The stability of vitamin D3 was significantly improved upon complexation with βlg. [•] The resistance of βlg to proteases in the intestines was improved. [•] The βlg/D3 complex crossed the Caco-2 cells monolayer. [•] The bioavailability of D3 was significantly increased upon binding to βlg. [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: 92874752 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Increased stability and protease resistance of the β-lactoglobulin/vitamin D<subscript>3</subscript> complex. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Diarrassouba%2C+Fatoumata%22">Diarrassouba, Fatoumata</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Garrait%2C+Ghislain%22">Garrait, Ghislain</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Remondetto%2C+Gabriel%22">Remondetto, Gabriel</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Alvarez%2C+Pedro%22">Alvarez, Pedro</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Beyssac%2C+Eric%22">Beyssac, Eric</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Subirade%2C+Muriel%22">Subirade, Muriel</searchLink><relatesTo>1</relatesTo><i> Muriel.Subirade@fsaa.ulaval.ca</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Food+Chemistry%22">Food Chemistry</searchLink>. Feb2014, Vol. 145, p646-652. 7p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Proteolytic+enzymes%22">Proteolytic enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Lactoglobulins%22">Lactoglobulins</searchLink><br /><searchLink fieldCode="DE" term="%22Vitamin+D%22">Vitamin D</searchLink><br /><searchLink fieldCode="DE" term="%22Chemical+stability%22">Chemical stability</searchLink><br /><searchLink fieldCode="DE" term="%22Complexation+reactions%22">Complexation reactions</searchLink><br /><searchLink fieldCode="DE" term="%22Bioavailability%22">Bioavailability</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Highlights: [•] The stability of vitamin D3 was significantly improved upon complexation with βlg. [•] The resistance of βlg to proteases in the intestines was improved. [•] The βlg/D3 complex crossed the Caco-2 cells monolayer. [•] The bioavailability of D3 was significantly increased upon binding to βlg. [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.2013.08.075 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 7 StartPage: 646 Subjects: – SubjectFull: Proteolytic enzymes Type: general – SubjectFull: Lactoglobulins Type: general – SubjectFull: Vitamin D Type: general – SubjectFull: Chemical stability Type: general – SubjectFull: Complexation reactions Type: general – SubjectFull: Bioavailability Type: general Titles: – TitleFull: Increased stability and protease resistance of the β-lactoglobulin/vitamin D3 complex. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Diarrassouba, Fatoumata – PersonEntity: Name: NameFull: Garrait, Ghislain – PersonEntity: Name: NameFull: Remondetto, Gabriel – PersonEntity: Name: NameFull: Alvarez, Pedro – PersonEntity: Name: NameFull: Beyssac, Eric – PersonEntity: Name: NameFull: Subirade, Muriel IsPartOfRelationships: – BibEntity: Dates: – D: 15 M: 02 Text: Feb2014 Type: published Y: 2014 Identifiers: – Type: issn-print Value: 03088146 Numbering: – Type: volume Value: 145 Titles: – TitleFull: Food Chemistry Type: main |
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