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Clostridium perfringens produced eight extracellular and two intracellular amylolytic activities when examined by zymograms following polyacrylamide gel electrophoresis under native conditions. The major intracellular amylase was isolated from vegetative cells of C. perfringens. It possessed an estimated molecular mass of 112 kDa. Sulfhydryl and phenol functional groups were essential to its activity. The amylase was endo-acting on starch and also hydrolyzed pullulan. Polyclonal antisera against a purified extracellular amylase did not cross-react with intracellular amylase and the two amylases were biochemically different. The distribution of extracellular amylolytic activities of sporulating cells was different from that of vegetative cells, whereas the distribution of intracellular amylolytic activities remained identical. A significant increase of a particular amylase (A8) occurred in the extracellular fluid during sporulation compared with that during vegetative growth. Regulation of the excretion of amylase(s) may be sporulation and enterotoxingenicity related.
N J Shih, and
R G Labbé
November 2011,
Microbial pathogenesis,
N J Shih, and
R G Labbé
June 1975,
The Journal of applied bacteriology,
N J Shih, and
R G Labbé
September 2002,
Journal of food protection,
N J Shih, and
R G Labbé
June 2016,
Microbiology spectrum,
N J Shih, and
R G Labbé
November 1972,
Applied microbiology,
N J Shih, and
R G Labbé
January 1969,
Annales de l'Institut Pasteur de Lille,
N J Shih, and
R G Labbé
January 2002,
Medycyna doswiadczalna i mikrobiologia,
N J Shih, and
R G Labbé
February 1999,
Letters in applied microbiology,
N J Shih, and
R G Labbé
May 1984,
Applied and environmental microbiology,
N J Shih, and
R G Labbé
March 1975,
Applied microbiology,
