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Selective separation of tryptic β‐casein peptides through ultrafiltration membranes: Influence of ionic interactions
Author(s) -
Nau F.,
Kerhervé F. L.,
Leonil J.,
Daufin G.
Publication year - 1995
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260460307
Subject(s) - isoelectric point , chemistry , membrane , chromatography , ultrafiltration (renal) , peptide , size exclusion chromatography , isoelectric focusing , ionic strength , casein , biochemistry , organic chemistry , aqueous solution , enzyme
Peptide separation by selective membrane filtration has numerous potential applications such as production of peptides with biological activities or spectific enrichment in compounds acting as flavoring agents or as growth factors required by the fermentation industry. The retention of peptides arising from tryptic hdroysis of β‐casein using an M5 Carbosep membrane (molecular wieght cutoll = 10,000 D) has been studied. The peptides with known sequences were characterized by their molecular weight, isoelectric point, and hydrophobicity. Our experiments highlighted that their transmission involves mechanisms other than size exclusion as developed elsewhere. The effect of ionic interactions between peptides and membrance has been investgated by vrying pH, ionic strength of bulk, and electric potential of filtering material. The charge of both peptides and membrane plays an important role in the transmission, particularly with small size and high or lkow isoelectric point. Then, peptides with the same sign as the membrane have lower transmission than expected from the size xclusion model, whereas peptides with opposite sign have higher trnsmission than expected, and even higher than 1 with some of them. © 1995 John Wiley & Sons, Inc.