Analysis of secreted protein profile and enzymatic activities from Corynebacterium diphtheriae and Bordetella pertussis on production batch media using peptide quenched fluorescent substrates

Analysis of secreted protein profile and enzymatic activities from Corynebacterium diphtheriae and Bordetella pertussis on production batch media using peptide quenched fluorescent substrates

Author Perpetuo, Elen Aquino Google Scholar
Lebrun, Ivo Google Scholar
Juliano, Luis Autor UNIFESP Google Scholar
Juliano, Maria Aparecida Autor UNIFESP Google Scholar
Sakauchi, Maria Aparecida Google Scholar
Prado, Sally M. A. Google Scholar
Institution Butantan Inst
Universidade Federal de São Paulo (UNIFESP)
Abstract Proteases were identified and characterized from the culture supernatant of the C. diphtheriae and B. pertussis bacteria. the proteases were secreted in the media and detected at the end of the exponential growth phase. Activity was detected in some fluorescent substrates, based on selected protein sequences such as insuline beta-chain, bradykinin, and synaptobrevin. the proteases were purified by means of gel filtration chromatography. Sodium dodecyl sulfate- polyacrylamide gel electrophoresis ( SDS- PAGE) analysis of the purified proteins indicated, for the main secreted proteins, an estimated molecular mass of 30 kDa in C. diphtheriae and 69 kDa in B. pertussis culture media. the proteases were stable and presented enzymatic activity at 378 degrees C. These proteases were not related to the main toxic compounds described in these two bacteria, but could represent good markers for the fermentation process when the enzyme activity was measured with the fluorescent substrates.
Keywords diphtheria toxin
pertussis toxin
fluorescent substrates
proteolytic activity
culture media
Language English
Date 2007-01-01
Published in Preparative Biochemistry & Biotechnology. Philadelphia: Taylor & Francis Inc, v. 37, n. 4, p. 353-367, 2007.
ISSN 1082-6068 (Sherpa/Romeo, impact factor)
Publisher Taylor & Francis Inc
Extent 353-367
Origin http://dx.doi.org/10.1080/10826060701593274
Access rights Closed access
Type Article
Web of Science ID WOS:000249781000005
URI http://repositorio.unifesp.br/handle/11600/29409

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