ALESSANDRA BASSO, BENJAMIN D SUMMERS^*, ROSIE JACKSON, SIMONA SERBAN, CHRISTOPHER BRESNER
*Corresponding author
Purolite Ltd., Llantrisant Business Park, Llantrisant, United Kingdom

Abstract

With the increasing demand for pure and cost-effective dairy proteins such as lactoferrin and lactoperoxidase, chromatographic methods need to provide efficient and scalable solutions for the purification of these high value proteins. In the present paper we compare three different resin technologies based on differing chemistries and analyse binding capacity and separation efficiency during purification of skimmed milk. Since the economics are a big driver in decisions during the design of new installations, an economic analysis considering a potential real plant requirement has been carried out and highlights the advantages and disadvantages of the three technologies.

DAIRY PROTEINS

Recently there has been an expansion in manufacture of isolated proteins obtained from dairy products such as milk and whey. Within milk and whey, there are a wide range of industrially interesting proteins, with applications ranging from nutrition to pharmaceutical and through to cosmetic uses (1, 2).

Summarised in Table 1 are several of the most well-known proteins from an industrial point of view. This complex mixture of proteins is challenging to separate completely, however the two proteins lactoferrin and lactoperoxidase can be readily separated by cation exchange chromatography (3). 

This possibility facilitates the use of an ‘added-value’ process in the treatment of whey, traditionally viewed as a waste product, thus valorising an otherwise unexploited source of high value commercial proteins.

Lactoferrin (LF) is a globular glycoprotein of approximately 700 amino acid residues with a molecular weight of about 78 kDa. The protein also has a relatively high isoelectric point (pI≈8.7) indicating that it is positively charged over a ...