Association behavior of native beta-lactoglobulin

M. Verheul, J.S. Pedersen, S.P.F.M. Roefs, K.G. de Kruif

    Research output: Contribution to journalJournal article

    Abstract

    The association behavior of beta-lactoglobulin has been studied by small-angle neutron scattering as a function of protein concentration, temperature, pH, and NaCl concentration of the solution. By indirect Fourier transformation of the spectra, pair-distance distribution functions for the various samples were obtained. These functions provided information on the maximum size, the weight-averaged molecular mass, and the z-averaged radius of gyration oo the the beta-lactoglobulin particles. Al room temperature and pH values below 4 and above IZ the protein consists predominantly of monomers and dimers, consistent with literature. In these pH regimes the formation of dimers is favored upon increasing ionic strength and decreasing protein charge (pH values closer to the isoelectric point of the protein). Around pH 4.7 larger oligomeric structures ape formed enhanced by a decrease in temperature and a decrease in ionic strength. beta-Lactoglobulin A associates more strongly than beta-lactoglobulin B. Surprisingly, at pH 6.9 larger structures than dimers seem to be formed at high protein concentrations (>30 mg mL(-1)). (C) 1999 John Wiley & Sons, Inc.
    Original languageEnglish
    JournalBiopolymers
    Volume49
    Issue number1
    Pages (from-to)11-20
    ISSN0006-3525
    Publication statusPublished - 1999

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