H+-ATPase activity in Bifidobacterium with special reference to acid tolerance.
The acid tolerance of 17 strains of nine species of bifidobacteria was compared using brief exposures to acidic conditions (pH 2-5). In addition, because it has been hypothesized that the acid tolerance of bifidobacteria depends on H+-ATPase activity, the activity of this enzyme in various strains and species was compared. In general, the acid tolerance of bifidobacteria was found to be weak, with the exception of Bifidobacterium lactis and Bifidobacterium animalis. High numbers of all strains of B. lactis and B. animalis survived exposure to pH 3-5 for 3 h. The H+-ATPase activity of the acid-tolerant strains B. lactis LKM512 and JCM 10602T, and B. animalis JCM 1190T, JCM 1253, JCM 7117, and JCM 7124 was higher at pH 4 than at pH 5. In contrast, the H+-ATPase activity of nonacid-tolerant strains was lower at pH 4 than at pH 5.
Matsumoto
Mitsuharu
M
Fundamental Research Laboratory, Kyodo Milk Industry Co. Ltd., 20-1 Hirai, Hinode, Tokyo 190-0182, Japan. m-matumoto@meito.co.jp
Ohishi
Hifumi
H
Benno
Yoshimi
Y
D000222:Adaptation, Physiological; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D001644:Bifidobacterium / Q000201:enzymology* / Q000502:physiology*; D015169:Colony Count, Microbial; D005511:Food Handling / Q000379:methods; D005516:Food Microbiology; D006863:Hydrogen-Ion Concentration; D015014:Yogurt / Q000382:microbiology
D000251:Adenosine Triphosphatases