Alcohol Determination in Protein Fractionation Intermediates by Steam Distillation and Digital Refractometry

by Heinz Anderle, Matthias Spork, David Horn, Theresa Bauer, Lucia Gnauer, and Alfred Weber
Volume 19, Open Access (May 2020)

Almost 75 years after implementing the industrial ethanol fractionation process, based on the pioneering work of Edwin J. Cohn’s research group, this niche biotechnology process has not lost its importance in helping to supply patients with life-saving biotherapies. Clearly, the focus has shifted from albumin, which was first used, to the indispensable immunoglobulin preparations produced for the effective, long-term treatment of patients suffering from immunodeficiencies. In addition, the widespread and safe therapeutic use of immunoglobulins has paved the way for the development of monoclonal antibodies, now used not only for the treatment of various autoimmune diseases, but also for cancer treatment. The Cohn fractionation process, based on the different solubilities of plasma proteins, depends on the five parameters of ethanol concentration, pH, temperature, protein, and salt concentration, which are the basis of this development. Ethanol concentration can clearly be considered an essential critical parameter for this process. Therefore, it is surprising that even after the advent of process analytical technology, there is still no fast, precise, and accurate procedure at hand to determine the alcohol content of Cohn fractionation intermediates. In this paper, we will describe the implementation of an old methodology for a new purpose, which is designed to close this gap.

Anderle H, Spork M, Horn D, Bauer T, Gnauer L, Weber A. Alcohol determination in protein fractionation intermediates by steam distillation and digital refractometry. BioProcess J, 2020; 19.

Posted online May 23, 2020.