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An improved and simplified method for the large‐scale purification of pediocin PA‐1 produced by Pediococcus acidilactici
Author(s) -
Beaulieu Lucie,
Aomari Hafida,
Groleau Denis,
Subirade Muriel
Publication year - 2006
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba20050041
Subject(s) - pediococcus acidilactici , bacteriocin , chemistry , preservative , chromatography , sepharose , pediococcus , antimicrobial , biochemistry , bacteria , lactobacillus , biology , organic chemistry , enzyme , lactic acid , fermentation , genetics , lactobacillus plantarum
The bacteriocin pediocin PA‐1 produced by Pediococcus acidilactici PAC 1.0 offers significant potential as a food preservative and as an antimicrobial agent in the medical area. However, low production yields and difficulties in obtaining significant amounts of pure pediocin PA‐1 have limited, in part, its biochemical and physical characterization. In the present study, we describe a simple and more efficient purification strategy for pediocin PA‐1. A hydrophobic interaction chromatography step using an octyl‐Sepharose column was introduced for final purification and polishing. The new method is a scalable one, uses only two steps and yields highly purified pediocin PA‐1 with a recovery as high as 73%, which is at least two to three times more than that of the methods reported so far. Highly purified, biologically active pediocin PA‐1 of the correct molecular mass (4624 Da, with two disulphide bridges) was obtained. Fourier‐transform infrared analysis runs at p 2 H 6 indicated that pediocin PA‐1 was more structured than similar pediocin PA‐1 samples purified using the earlier purification scheme.