Fractal analysis of structure of beta-lactoglobulin preparations.
Beta-lactoglobulin (beta-Lg) preparations obtained from whey retentate through (a) salting out at high NaCl concentration in a strongly acid medium (30% NaCl, pH 2.0), (b) alfa-lactalbumin (alfa-La) removal at mild conditions (55 degrees C/30 min, pH 3.9) and (c) alfa-La removal with 6% TCA solutions (20 degrees C/40 min) were characterized by high values (1.31 to 1.33) for fractal dimension (D(L)), indicating their developed surface. At the same time, a small differentiation between these values allows assuming that the methods of the protein isolation from whey retentate did not influence the surface development. High values for correlation coefficients indicated a great accuracy of the method used for the measurements of the protein particles.
J
J
Leman
M
M
Smoczyski
T
T
Doga
Z
Z
Dziuba
D005504:Food Analysis / Q000379:methods*; D017709:Fractals; D007091:Image Processing, Computer-Assisted / Q000379:methods*; D007782:Lactoglobulins / Q000737:chemistry / Q000648:ultrastructure*; D008855:Microscopy, Electron, Scanning / Q000379:methods*
D007782:Lactoglobulins