Lipase and Esterase Activities of Propionibacterium freudenreichii subsp. freudenreichii

AUTOR(ES)

Dupuis, C.

RESUMO

The lipase and esterase activities of eight strains of dairy Propionibacterium freudenreichii subsp. freudenreichii were studied. A lipase activity was detected on whole cells and in the culture supernatant. The highest activity was expressed at 45°C and pH 6.8. An esterase activity was also detected in the culture medium. The electrophoresis of the intracellular fractions of the cells revealed from three to six different esterase activities. Two esterases were common to all the strains. The substrate specificity was dependent on each esterase, but no activity was revealed, in our experimental conditions, on ester substrates with a chain length longer than that of butyrate.

Documentos Relacionados

• First Evidence of Lysogeny in Propionibacterium freudenreichii subsp. shermanii
• Properties of Alanine Dehydrogenase and Aspartase from Propionibacterium freudenreichii subsp. shermanii
• Enhanced Propionate Formation by Propionibacterium freudenreichii subsp. freudenreichii in a Three-Electrode Amperometric Culture System
• Metabolism of Aspartate by Propionibacterium freudenreichii subsp. shermanii: Effect on Lactate Fermentation
• Citrate Cycle Intermediates in the Metabolism of Aspartate and Lactate by Propionibacterium freudenreichii subsp. shermanii