We are happy for our new publication on the characteristics of LACTOFERRIN in the journal PROCESSES

We have published the results of initial pilot research within the LIFE for Acid Whey project in the field of characterization of lactoferrin - a whey protein isolated from acid whey.

The aim of this study was to characterize the properties of lactoferrin (LF) obtained in a process developed for its isolation from acid whey derived from the production of fresh curd cheese, using a unique technology of ion-exchange chromatography on CIM® monolithic columns. The freeze-dried lactoferrin samples produced on the pilot plant (capacity 1 m3) were examined for the purity, iron-binding capacity, antibacterial activity, and pH- and temperature-stability. Apo-LF inhibited several tested strains (enterobacteria, Staphylococcus, Streptococcus salivarius) except clostridia, lactic acid bacteria, and bifidobacteria. Sample of LF intentionally saturated with Fe3+ lost its antibacterial activity, indicating the involvement of mechanisms based on depriving bacteria of an iron source. All samples, regardless of the iron-saturation level, exhibited stability in pH range 4.0 to 11.0. LF with higher iron content (A-value = 41.9%) showed better thermal stability. Heat treatment up to 72 °C/3 s did not reduce antimicrobial activity against E. coli O157: H7 tox-. Higher purity (above 91%), higher iron-binding capacity and higher inhibitory activity against E. coli O157: H7 tox- compared to some similar products from the market was observed. These results demonstrate a high potential of monolithic ion-exchange chromatography for industrial processing of acid whey as a source of LF that can be used in new products with high-added value. The upscaling of the process is ongoing on a demonstration plant (10–30 m3/day capacity).

The article entitled “Characterization of Lactoferrin Isolated from Acid Whey Using Pilot-Scale Monolithic Ion-Exchange Chromatography” is available at the following link.