Premium
Proton‐ATPase activity in cells of lactobacilli grown in the presence of propionate
Author(s) -
Chaia Adrians Pérez,
Strasser de Saad Ana M.,
de Ruiz Holgado Aída A. Pesce,
Oliver G.
Publication year - 1994
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1994.tb03041.x
Subject(s) - propionate , lactobacillus casei , atpase , enzyme , biochemistry , substrate (aquarium) , enzyme assay , chemistry , biology , fermentation , ecology
Lactobacillus helveticus ATCC 15009 and CRL 581, and Lact. casei LC3 were grown in a complex medium with and without 15 mmol 1 ‐1 of neutralized propionic acid and assayed for proton‐translocating ATPase activity. The enzyme activity was higher when the medium contained fatty acid than in its absence for all strains studied. Characteristics of this increased ATPase were identical to those of the enzyme located on the membrane of normal cells. The substrate consumption rate of resting cells was increased by propionate. This effect was reverted by the specific H + ‐ATPase inhibitor N,N '‐dicyclohexylcarbodiimide indicating that the increment of fermentative activity was related to the H + ‐ATPase activity. These results suggest that the amplification of H + ‐ATPase activity could be involved in the inhibition of lactobacilli growth in cultures where propionic acid is unavoidably present, such as some mixed cultures with propionibacteria.