Method for the production of antibacterial peptides from biological fluids at an ionic membrane. Application to the isolation of nisin and caprine lactoferricin
| Autor: | Servaas Visser, Charles J. Slangen, Isidra Recio |
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| Rok vydání: | 2000 |
| Předmět: | |
| Zdroj: | ResearcherID |
| ISSN: | 1297-9694 0023-7302 |
| DOI: | 10.1051/lait:2000118 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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