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Author: search.filters.author.Chen, W. L.Subject: search.filters.subject.beta-lactoglobulin

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Now showing 1 - 4 of 4
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    A novel two-dimentional gel electrophoresis for studing the cress-linking between beta-Lactoglobulin and milk proteins
    (2005-01-01)
    Chen, W. L.
    ;
    Huang, M. T.
    ;
    Mao, S. J. T.
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    交大名義發表
    ;
    National Chiao Tung University
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    Item type:Item,
    Distinguish between native and thermally denatured 5-lactoglobulin using a monoclonal antibody as a probe.
    (2005)
    Mao, S. J. T.
    ;
    Chen, W. L.
    ;
    Yang, M. C.
    ;
    Liu, W. T.
    ;
    交大名義發表
  • Thumbnail Image
    Item type:Item,
    Distinguish between native and thermally denatured beta-lactoglobulin using a monoclonal antibody as a probe
    (2005)
    Mao, S. J. T.
    ;
    Chen, W. L.
    ;
    Yang, M. C.
    ;
    Liu, W. T.
    ;
    交大名義發表
  • Thumbnail Image
    Item type:Item,
    Antioxidant nature of bovine milk beta-lactoglobulin
    (2007-02-01)
    Liu, H. C.
    ;
    Chen, W. L.
    ;
    Mao, S. J. T.
    ;
    生物科技學系
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    Department of Biological Science and Technology
    Heating is necessary for processing milk in the dairy industry, which evidently produces a conformational change in beta-lactoglobulin (beta-LG). beta-Lactoglobulin, a major protein that accounts for approximately 10 to 15% of total milk proteins, is a globular protein consisting of 162 AA with a relative molecular mass of 18.4 kDa. The purpose of the present study was to determine the antioxidant role of beta-LG in milk and the possible mechanism involved. We showed that beta-LG is a mild antioxidant whose potency is less than that of vitamin E and probucol (the latter being an antioxidant used for clinical therapy). The conversion of the beta-LG monomer to dimer was responsible, in part, for the mode of action in protecting low- density lipoproteins against copper-induced oxidation. Cross-linking the free thiol groups of beta-LG by heating (100 degrees C for 2 min), or chemically modifying the beta-LG by carboxymethylation to block the thiol groups resulted in a substantial loss of antioxidant activity. The data suggest that Cys-121 plays an essential role in the antioxidant nature of beta-LG. By using an anti-LG antibody affinity column to deplete the beta-LG from milk, we observed from the lost antioxidant activity that beta-LG contributes approximately 50% of the total activity. Because beta-LG is extremely sensitive to thermal denaturation, to maintain its antioxidant nature, dairy products consumed daily should not be overheated in order to maintain its antioxidant nature.