Selective isolation of cationic amino acids and peptides by electro-membrane filtration

Abstract

International audienceIn the food industry there is a clear trend towards the production of speciality products with a high added value. Electro-membrane filtration (EMF) can be used to separate and concentrate these products from complex solutions. With EMF, lysine was separated from a model solution and a protein hydrolysate both containing leucine. The lysine fraction in the permeate ranged from 0.86 to 0.96. The lysine transport rate and purity were improved by increasing the potential difference from 20 V to 40 V. Reduction of the transmembrane pressure from 2 to 0.5 bar improved the purity at a practically unchanged lysine transport rate. An enriched fraction of antibacterial cationic peptides (e.g. lactoferricin-B) could be produced from a lactoferrin hydrolysate using EMF. Isolation of these bioactive peptides is normally expensive due to the complex nature of the hydrolysate feed. EMF has the potential to become an attractive (partial) isolation technology

Antibacterial activity of peptides extracted from tryptic hydrolyzate of whey protein by nanofiltration

“…A notable exception is the study of bovine lactoferricin (LfcinB), which has been purified using chromatography or other technological approaches applicable at an industrial scale (Bargeman, Dohmen-Speelmans, Recio, Timmer, & Van Der Horst, 2000;Pihlanto-Leppälä et al, 1999;Recio & Visser, 1999;Tomita et al, 1992;Visser & Recio, 1998). The study of materials obtainable by processes used in the dairy industry remains scant.…”

Advancements in the Fractionation of Milk Biopeptides by Means of Membrane Processes

“…In this sense, two different configurations can be distinguished: electrically-enhanced filtration, which can be used with conventional pressure driven membrane filtration, and forced-flow membrane electrophoresis, which is conducted in an electrophoretic cell. Intensive researches on these membrane processes have been carried out including electromembrane filtration (EMF) [94][95], electrodialysis with UF membranes (EDUF) [96][97][98][99] and forced-flow electrophoresis (FFE) [100] for the separation of charged bioactive molecules.…”

Selective separation of cationic peptides from a tryptic hydrolysate of β‐lactoglobulin by electrofiltration

“…The inter-electrode distance was 0.003 m. No protection of the electrodes by ion-exchange membranes was supplied. Inconsistent results are found in literature regarding electrolytic reactions during EF, even when electrodes are protected (Bargeman et al, 2000(Bargeman et al, , 2002. The DC power supply was a 0-100 V:0-10 A model XHR from Xantrex (Vancouver, BC, Canada).…”

“…However, only a few studies have focused at the use of EF in peptide fractionation. Daufin et al (1995) and Bargeman et al (2000Bargeman et al ( , 2002 used EF to fractionate cationic/basic peptides contained in protein hydrolysates prepared from b-casein, lactoferrin, and a S2 -casein. In these studies, the selective transmission of basic peptides in permeate was obtained by inserting the cathode (À) on the permeate side in order to facilitate their transport from the feed stream.…”