Bioactive peptides recovery

The simultaneous separation and recovery of acidic and basic bioactive peptides by employing electrodialysis with ultrafiltration membranes has also been investigated recently [30]. This work aims at demonstrate the feasibility of separating peptides from a beta-lactoglobulin hydrolysate, using an ultrafiltration membrane stacked in an electrodialysis cell, and a study of the effect of pH on the migration of basic/ cationic and acid/anionic peptides in the electrodialysis configuration. 

Kitts, D. D., and Weiler, K. 2003. Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery. Curr. Pharma. Design, 9,1309-1323. 

Fig. 4 Self-assembling hydrogelators based on p-sheets. (a) Representative chemical structure of a peptide amphiphile, here without charged residues and with a heparin binding domain, (b) Peptide amphiphile with bioactive epitopes left) and its assembly leading to formation of ID fibers right). Reprinted from [136], Copyright 2010, with permission from Elsevier, (c) Graph showing the enhanced functional recovery for animals treated with the peptide amphiphile, as assessed via the BBB score. Adapted with permission from [78]. Copyright 2008 Society for...

Inherent in all RPC and HlC investigations with peptides or proteins is the question of the end use to which the separated products will be applied. If the task involves purification solely for subsequent primary structure determination (i.e., essentially an analytical task at a semi-preparative scale), then control over preservation of bioactivity may not be necessarily relevant. Obviously, with a new or partially characterized protein, recovery of the component of interest with high mass and bioactivity balance is essential. For preparative methods where subsequent biological uses are contemplated, it is similarly mandatory that the design of the RPC or HlC separation system specifically address recovery issues. High recovery of bioactivity can usually be satisfied without sacrificing the obvious demands of selectivity through proper attention to the physicochemical consequences of the dynamic behavior of the polypeptide or protein of interest in bulk solution and at liquid-solid interfaces. 

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