Design Considerations for the Batch Capture of Proteins from Raw Whole Milk by Ion Exchange Chromatography

Abstract

Batch extraction of proteins directly from raw, whole milk is described with a focus on design considerations for on-farm implementation. A demonstration of single-stage stirred tank extraction of bovine lactoferrin onto cation exchangers shows that processing can be achieved, with no pre-treatment of raw milk, within the timeframe required to milk an On-farm extraction of proteins shows promise for both the production of minor, high-value proteins from conventional milk and for production of recombinant proteins from the milk of transgenic animals. The main advantage of the stirred tank process is that protein extraction is rapid and is achieved in a single step without the need for pre-treatment of milk. The process is not limited to ion exchange but could be implemented using other chromatographic techniques, such as affinity or reverse-phase chromatography.2

Sulfanilic acid‐modified chitosan mini‐spheres and their application for lysozyme purification from egg white

“…For this reason, 100 mg matrix per 1 mL egg white was the quantity of matrix chosen for further studies. In a previous work, Fee and Chand established that there was a given value for the relation between the sample volume and the matrix amount, in which by increasing the matrix quantity there was no increase in the target protein bound to it, but there was a reduction of the time required to complete the adsorptive step. This effect was also verified in a previous work published by Baieli et al on lactoferrin purification from sweet whey.…”