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 of the beta-lactoglobulin particles. At room temperature and pH values below 4 and above 5.2 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 are 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).
journal_name
Biopolymersjournal_title
Biopolymersauthors
Verheul M,Pedersen JS,Roefss SP,de Kruif KGdoi
10.1002/(SICI)1097-0282(199901)49:1<11::AID-BIP2>3subject
Has Abstractpub_date
1999-01-01 00:00:00pages
11-20issue
1eissn
0006-3525issn
1097-0282pii
10.1002/(SICI)1097-0282(199901)49:1<11::AID-BIP2>3journal_volume
49pub_type
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