Abstract
Publisher Summary This chapter presents that parallel strands of work concerned with the quality of beer foams and the positive recovery of proteins from complex feedstocks by foaming has indicated a role for the study of the foaming behavior of well-defined single- and two-component protein solutions. Such solutions are representative of real systems and are characterized by quantifiable foam qualities. Understanding the molecular interactions in these systems is essential to the development of controlled foam fractionation as a separation unit in downstream processing. Foam stability of homogeneous and heterogeneous feedstocks is measured as the Head Retention Value (HRV)—namely, the foam half-life, by the application of the Rudin method. The homogeneous preparations studied in the chapter contain Bovine Serum Albumin (BSA), an acidic protein (pi 4.8) of molecular mass 6.7 ×104 daltons. The chapter examines the influence of BSA concentration, pH conditions (pH 3.2-6.2), and salt concentration upon the head retention value. It concludes that foam stability of a heterogeneous protein solution is enhanced when pH conditions favor electrostatic interactions between acidic and basic proteins. In addition, when electrostatic attractions are suppressed by addition of salt and interactions of hydrophobic nature are expressed, the foam stability of the heterogeneous systems becomes more greatly enhanced.
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