Variability and molecular typing of Streptococcus thermophilus strains displaying different proteolytic and acidifying properties

Proteolytic and acidifying properties of Streptococcus thermophilus strains isolated from yoghurt or cheeses were evaluated. Among 30 strains tested, 12 exhibited cell envelope-associated proteinase activity (PrtS+), three displayed a slight PrtS activity (PrtS+/−) and 15 were PrtS−, despite the presence of the corresponding gene (prtS) in eight of them. Sequencing of the prtS gene in four PrtS− and one PrtS+ strains revealed that the absence of PrtS activity in the PrtS− strain probably results from an alteration of the prtS regulation. The strains displaying the highest acidifying capacities were all PrtS+. All but one PrtS+ strains were phylogenetically close, as shown by the sequencing of their rDNA internal transcribed spacer (ITS) 16S-23S. More specifically, the high proteolytic and acidifying capacities are associated with the presence of a type II-ITS.