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 D3 complex.
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
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DbLabel: Engineering Source
An: 92874752
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PubType: Academic Journal
PubTypeId: academicJournal
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  Data: Increased stability and protease resistance of the β-lactoglobulin/vitamin D<subscript>3</subscript> complex.
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  Data: <searchLink fieldCode="JN" term="%22Food+Chemistry%22">Food Chemistry</searchLink>. Feb2014, Vol. 145, p646-652. 7p.
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  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>
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  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]
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  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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      – Type: doi
        Value: 10.1016/j.foodchem.2013.08.075
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      – Code: eng
        Text: English
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        PageCount: 7
        StartPage: 646
    Subjects:
      – SubjectFull: Proteolytic enzymes
        Type: general
      – SubjectFull: Lactoglobulins
        Type: general
      – SubjectFull: Vitamin D
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      – SubjectFull: Chemical stability
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      – SubjectFull: Complexation reactions
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      – SubjectFull: Bioavailability
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      – TitleFull: Increased stability and protease resistance of the β-lactoglobulin/vitamin D3 complex.
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            NameFull: Garrait, Ghislain
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              Text: Feb2014
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