Lipase and Esterase Activities of Propionibacterium freudenreichii subsp. freudenreichii

Lipase and Esterase Activities of Propionibacterium freudenreichii subsp. freudenreichii.

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 degrees C and pH 6.8. An esterase activity was also detected in the culture medium. The electrophoresis of the intracellular fractions of the cells ...

Aminopeptidase activities of Propionibacterium freudenreichii dairy isolates

This study was undertaken to achieve more information on the aminopeptidase activities expressed in Propionibacterium freudenreichii strains naturally occurring in milk and dairy products. Fifty four strains belonging to both subspecies freudenreichii and shermanii were analyzed for activity towards different amino acyl β-naphthylamide (βNA) derivatives. The ability to efficiently hydrolyze ami...

Enhanced Propionate Formation by Propionibacterium freudenreichii subsp. freudenreichii in a Three-Electrode Amperometric Culture System.

In order to influence the fermentation pattern of Propionibacterium freudenreichii towards enhanced propionate formation, growth and product formation with glucose and lactate as energy sources were studied in a three-electrode poised-potential amperometric culture system. With anthraquinone 2,6-disulfonic acid (E(0)' = -184 mV; poised electron potential = -224 mV) or cobalt sepulchrate (E(0)' ...

Utilization of coenzyme A by Propionibacterium freudenreichii.

Properties of Alanine Dehydrogenase and Aspartase from Propionibacterium freudenreichii subsp. shermanii.

During lactate fermentation by Propionibacterium freudenreichii subsp. shermanii ATCC 9614, the only amino acid metabolized was aspartate. After lactate exhaustion, alanine was one of the two amino acids to be metabolized. For every 3 mol of alanine metabolized, 2 mol of propionate, 1 mol each of acetate and CO(2), and 3 mol of ammonia were formed. The specific activity of alanine dehydrogenase...