Free Access
| Issue |
Lait
Volume 80, Number 1, January-February 2000
New applications of membrane technology in the dairy industry
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| Page(s) | 187 - 195 | |
| DOI | https://doi.org/10.1051/lait:2000118 | |
DOI: 10.1051/lait:2000118
Lait 80 (2000) 187-195
Method for the production of antibacterial peptides from biological fluids at an ionic membrane. Application to the isolation of nisin and caprine lactoferricin
Isidra Recio, Charles J. Slangen, Servaas Visser
Department of Product Technology, NIZO food research, P.O. Box 20, 6710 BA Ede, The Netherlands
Abstract:
Cationic peptides could be successfully released from a precursor protein bound to a cation-exchange
membrane by in-situ enzymatic cleavage with an appropriate enzyme. This procedure allows the washing-off
of other hydrolytic fragments from the membrane before the selective removal of the strongly bound target
peptide(s) at increased pH or with high ionic strength buffer. Two new applications of this method are
presented. The lantibiotic nisin could be released with high efficiency by tryptic hydrolysis of its
precursor polypeptide bound to the ionic membrane. Further, the production of a fraction enriched in a
novel antibacterial domain from the N-terminal part of caprine lactoferrin is reported. Characterisation
of this domain by mass spectrometry and N-terminal sequence analysis revealed that this peptide
corresponded to fragment 14-42 of the sequence of mature caprine lactoferrin, here referred to as
lactoferricin-C. Thus, the purification procedure shown can be used to isolate cationic peptides initially
produced in a longer, inactive form by bacteria (fusion proteins) or naturally occurring antibacterial
peptides generated by the digestion of proteins.
antibacterial cationic peptide / membrane cation-exchange chromatography / hydrolysis of membrane-bound protein / nisin / caprine lactoferricin
Correspondence and reprints: S. Visser
SVISSER@nizo.nl
Copyright INRA, EDP Sciences