• Login
    View Item 
    •   T-Stór
    • Food Programme
    • Food Chemistry & Technology
    • View Item
    •   T-Stór
    • Food Programme
    • Food Chemistry & Technology
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of T-StórCommunitiesPublication DateAuthorsTitlesSubjectsFunderThis CollectionPublication DateAuthorsTitlesSubjectsFunderProfilesView

    My Account

    LoginRegister

    Information

    Deposit AgreementLicense

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    The influence of bovine serum albumin on β-lactoglobulin denaturation, aggregation and gelation

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    Publisher version
    View Source
    Access full-text PDFOpen Access
    View Source
    Check access options
    Check access options
    Thumbnail
    Name:
    Kehoe Morris Brodkorb _2007_ ...
    Size:
    463.5Kb
    Format:
    PDF
    Download
    Author
    Kehoe, Joseph James
    Morris, Edwin R
    Brodkorb, Andre
    Keyword
    β-lactoglobulin
    Denaturation
    Bovine Serum Albumin
    Thiol groups
    Kinetics
    Gelation
    Date
    22/11/2006
    
    Metadata
    Show full item record
    Statistics
    Display Item Statistics
    URI
    http://hdl.handle.net/11019/513
    Citation
    Kehoe, J. J., Morris, E. R., & Brodkorb, A. (2007). The influence of bovine serum albumin on [beta]-lactoglobulin denaturation, aggregation and gelation. Food Hydrocolloids, 21(5-6), 747-755. DOI: 10.1016/j.foodhyd.2006.10.001
    Abstract
    The effect of bovine serum albumin (BSA) on the heat-induced denaturation, aggregation and subsequent acid-induced gelation of β-lactoglobulin (β-lg) was investigated in this work. Changes in the denaturation kinetics of β-lg during heating at 78 °C were determined by monitoring the disappearance of the native protein by reverse-phase chromatography. Replacing β-lg with increasing amounts of BSA, while keeping the total protein concentration constant at 5% (w/w), significantly increased the denaturation rate of β-lg from 2.57±0.30×10−3(g L−1)(1−n)s−1 to 5.07±0.72×10−3(g L−1)(1−n)s−1 (β-lg: BSA ratio of 3:1 w/w). The reaction order for β-lg was 1.40±0.09. Partial replacement of β-lg with BSA (β-lg: BSA ratio of 3:1 w/w) significantly increased the reaction order to 1.67±0.13. Heat-induced aggregates between β-lg and BSA were studied by dynamic light scattering, two-dimensional electrophoresis and size exclusion chromatography. The partial replacement of β-lg with BSA significantly changed the gelling properties of the acid-induced gels. A rapid rate of acidification resulted in a significant decrease, while a slow acidification rate resulted in a significant increase in gel strength. Size exclusion chromatography demonstrated that intermolecular disulphide bond formation occurred during both heat-induced denaturation/aggregation and subsequent acid-induced gelation. Results clearly indicate that BSA contributed to the formation of these disulphide bonds.
    Funder
    Department of Agriculture, Food and the Marine; Teagasc Walsh Fellowship Programme
    ae974a485f413a2113503eed53cd6c53
    http://dx.doi.org/10.1016/j.foodhyd.2006.10.001
    Scopus Count
    Collections
    Food Chemistry & Technology
    Food Chemistry & Technology

    entitlement

     
    DSpace software copyright © 2002-2017  DuraSpace
    Quick Guide | Contact Us | Send Feedback
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.