Abstract
Sedimentation and titration behavior of goat β-lactoglobulin has been compared with those of bovine and buffalo β-lactoglobulins. In sedimentation, goat, bovine, and buffalo β show close similarity. Titrations in the pH range 2–10, in the presence of formaldehyde and at two temperatures show that titration and analytical results of goat β do not agree. Goat β, similar in amino acid composition to cow β-B, has four nontitratable carboxyl groups as shown by amide nitrogen estimation and titration of denatured protein. Nonlinearity of logarithmic plots according to Linderstrøm-Lang equation in the acid region at different ionic strengths and effect of neutral salt on the isoionic pH show goat β to be conformationally different from cow β-B. Experimental and computed curves fit above pH 4 with a single value of the electrostatic interaction parameter w by assuming two sets of carboxyls with different p K values. A lower value of w has been assumed below pH 4 to fit the curve and suggests expansion of the molecule.
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