Influence of salts on selective coagulation of whey proteins and their application in the isolation of β-lactoglobulin

Abstract

Hanušová J., Mihulová M., Diblíková L., Čurda L. (2014): Influence of salts on selective coagulation of whey proteins and their application in the isolation of β-lactoglobulin. Czech J. Food Sci., 32: 77-81.Whey proteins are an important constituent of milk, especially whey from cheese manufacture and have many valuable functional properties such as foaming and emulsifying ability or gel formation. Some whey proteins are sensitive to salt content in a solution. High or low salt content may lead to selective coagulation of these proteins. A part of whey proteins was precipitated by addition of 7% (wt) NaCl and β-lactoglobulin and caseinomacropeptide remained in the supernatant. It was necessary to demineralise the supernatant by electrodialysis for the selective coagulation of caseinomacropeptide from this material. Subsequently, ethanol was added and pH was adjusted. This reduction of the ionic strength and the addition of ethanol induced the selective precipitation of caseinomacropeptide (91.4% from the original amount of CMP). β-lactoglobulin of 91% purity remained in the solution.

Peptic treatment of beta-lactoglobulin improves foaming properties substantially

“…The β‐Lg content increased from 64 to 81% (WPC) and from 55 to 89% (WPI) in the enriched product, respectively. Hanusova, Mihulova, Diblikova, and Curda () developed a process where a part of whey proteins was precipitated by adding 7% sodium chloride, while β‐Lg remained in the supernatant. Further process steps led to a β‐Lg isolate with purity greater than 90%.…”