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Production, purification et caracterisation de la pediocine PA-1 naturelle et de ses formes recombinantes: Contribution a la mise en evidence d'une nouvelle activite biologique (French and English text)

Posted on:2005-12-07Degree:Ph.DType:Dissertation
University:Universite Laval (Canada)Candidate:Beaulieu, LucieFull Text:PDF
GTID:1450390008488031Subject:Chemistry
Abstract/Summary:
Pediocin PA-1 is an antimicrobial peptide of interest in the food biopreservation field. Its exploitation is, however, limited due in part to its low production yield. In order to support additional studies on pediocin PA-1, an improved purification process, both simple and easily scalable, was proposed. This process served also as a basis for the purification of recombinant pediocins produced by expression systems derived from Pichia pastoris and Escherichia coli. Characterization of the recombinant pediocins has demonstrated that the recombinant pediocin from P. pastoris could be covalently bound to a "collagen-like" material whereas the recombinant pediocin from E. coli possessed properties very similar to those of the natural peptide. The cumulative work performed throughout this project has led to evaluation of the potential anticancer activity of natural pediocin PA-1 and to the observation that pediocin PA-1 possesses an important inhibitory activity against both lung and colon carcinoma human cell lines.
Keywords/Search Tags:Pediocin PA-1, Recombinant, Purification
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