ESTERASE-ACTIVITY OF DAIRY PROPIONIBACTERIUM

This paper reports results on the esterolytic activity of dairy Propio nibacterium. All the species present an active esterolytic system on n aphthyl substrates for fatty acids which contain < 10 carbons. Between 1 to 4 activities of different specificities were revealed on non-den aturing polyacrylamide gel electrophoresis for each species. These act ivity patterns could be very useful in differentiating between a few P ropionibacterium species. Ion-exchange chromatography allowed 3 main e sterase activities to be separated on a concentrated intracellular ext ract of P freudenreichii subsp freudenreichii. These activities have v ery different substrate specificities which agree closely with those d etermined by electrophoresis.