Proteolytic activity of streptococcus bovis cultured alone or associated with Prevotella albensis, on two kinds of protein substrates: Casein or pea proteins
M. Sales-duval et al., Proteolytic activity of streptococcus bovis cultured alone or associated with Prevotella albensis, on two kinds of protein substrates: Casein or pea proteins, ANAEROBE, 7(4), 2001, pp. 199-208
This work aims at studying in detail, the interaction between two major bac
terial species involved in the ruminal proteolysis, Streptococcus bovis and
Prevotella albensis. We chose to investigate this interaction by examining
their behaviour both alone in monoculture and together in co-culture on tw
o kinds of protein substrates. Comparison of the behaviour of S. bovis and
P. albensis in monoculture, in terms of growth and total proteolytic activi
ty with protein as the sole source of nitrogen, showed that S. bovis grew m
ore rapidly and developed a higher total proteolytic activity A higher prop
ortion of short peptides was generated at the end of the exponential growth
phase on pea protein medium whereas peptide accumulation did not appear on
casein medium for both species; peptides of casein origin would be used mo
re by species in monoculture than those of pea origin. S. bovis predominate
d in number in both co-cultures but the balance between species was greater
on pea proteins (S. bovis: 64% and P. albensis: 36%) than on casein (S. bo
vis: 86% and P. albensis: 14%). At the same time, the decrease of the prote
olytic activity was smaller on pea protein medium than that with casein and
the use of proteolysis products was facilitated; peptides liberated by pea
protein hydrolysis accumulated less than those obtained from casein. Moreo
ver, the diversity of the endopeptidases. expressed increased on pea protei
ns and the exopeptidase activities remained rather constant whereas they we
re highly stimulated on casein medium. All the results obtained in co-cultu
re on pea proteins allowed us to suggest that a greater synergism occurred
between the two species for the breakdown of proteins. (C) 2001 Academic Pr
ess.