Nl. Heredia et al., ALTERATION IN SPORULATION, ENTEROTOXIN PRODUCTION, AND PROTEIN-SYNTHESIS BY CLOSTRIDIUM-PERFRINGENS TYPE-A FOLLOWING HEAT-SHOCK, Journal of food protection, 61(9), 1998, pp. 1143-1147
Application of a heat shock (43 to 50 degrees C) applied early during
the sporulation process of Clostridium pelfringens delayed spore and e
nterotoxin production. Final levels of heat-resistant spores were simi
lar to the control, but enterotoxin levels were reduced when the heat
shock was applied at the third hour of incubation. The response of the
microorganism to the heat shock was also examined by analysis of puls
e-labeled proteins. Seven heat shock proteins (HSPs) associated with v
egetative cells were identified by polyacrylamide gel electrophoresis.
Most were localized mainly in the membrane, although one small protei
n was mostly present in the cytoplasm. Fewer HSPs were detected during
sporulation. Two HSPs were immunologically related to the GroEL and D
naK HSPs from Lactobacillus lactis and Escherichia coli, respectively.