Separation of bioactive peptides by Membrane processes : technologies and devices

ISSN: 2212-4012 (Online)
ISSN: 1872-2083 (Print)

Volume 8, 3 Issues, 2014

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Rongling Wu
Departments of Public Health Sciences and Statistics
Pennsylvania State College of Medicine
Hershey, PA

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Separation of bioactive peptides by Membrane processes : technologies and devices

Author(s): Laurent Bazinet

Affiliation: des Nutraceutiques et des Aliments Fonctionnels (INAF), Dairy Research Center (STELA), département des sciences des aliments et de nutrition, Université Laval, Québec, Canada G1V 0A6.


Although many patents reported bioactive peptides with numerous demonstrated bioactivities and potential applications, there exist some limitations to the production of large quantities to satisfy the growing market demands. Indeed, considering that most functional peptides are present in complex matrices containing a large number of hydrolyzed protein fractions, their separation and purification are required. Some advances have been made in the use of conventional pressure-driven processes for the continuous production and separation of peptides, however, most of these patented technologies are not scalable and demonstrate a low selectivity when separating similar sized biomolecules. To improve the separation efficiency, the use of an external electric field during pressure-driven filtration was proposed and patented. However, whatever the claims, the pressure gradient brings about the accumulation of peptides at the nearby membrane surface and affects the membrane transport selectivity. To overcome these drawbacks, a recent patent proposed the simultaneous fractionation of acidic and basic peptides, using a conventional electrodialysis cell, in which some ion exchange membranes are replaced by ultrafiltration ones. The perspectives in the field of peptide separation will be the development of new membrane materials and new equipments such as microfluidic devices to improve selectivity and yield of production.

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Article Details

Volume: 7
First Page:
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DOI: 10.2174/18722083113079990002

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