Abstract
Deposits formed on the membrane during ultrafiltration of aqueous solutions of individual whey proteins were examined under a scanning electron microscope. Gamma-globulin formed granules which agglomerated and stacked into layers to form a porous matrix on the membrane. Beta-lactoglobulin and bovine serum albumin both formed sheets on the membrane and formed multimers which were identified by sodium dodecyl sulfate gel electrophoresis. Beta-lactoglobulin also formed strands where deposits were not thick. Alpha-lactalbumin formed smooth spherical particles which did not hinder water permeation greatly. Studies of ultrafiltration rate indicated that beta-lactoglobulin and gamma-globulin were most significant in causing permeation flux decline by surface fouling.
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