Relationship Between Oxygen Sensitivity and Oxygen Metabolism of Bifidobacterium Species

Bifidobacteria, which are obligate anaerobes, were studied to determine the relationship between their sensitivity to oxygen and oxygen metabolism. Among the four species tested, Bifidobacterium infantis, Bifidobacterium breve, and Bifidobacterium longum differed from Bifidobacterium adolescentis in...

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Published inJournal of dairy science Vol. 75; no. 12; pp. 3296 - 3306
Main Authors Shimamura, Seiichi, Abe, Fumiaki, Ishibashi, Norio, Miyakawa, Hiroshi, Yaeshima, Tomoko, Araya, Tomoko, Tomita, Mamoru
Format Journal Article
LanguageEnglish
Published Savoy, IL Elsevier Inc 01.12.1992
Am Dairy Sci Assoc
American Dairy Science Association
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Summary:Bifidobacteria, which are obligate anaerobes, were studied to determine the relationship between their sensitivity to oxygen and oxygen metabolism. Among the four species tested, Bifidobacterium infantis, Bifidobacterium breve, and Bifidobacterium longum differed from Bifidobacterium adolescentis in sensitivity to oxygen. The former three species showed marked growth under conditions of partial aeration, whereas the growth of B. adolescentis was suppressed by low concentrations of oxygen. Bifidobacteria express reduced NAD-oxidase and -peroxidase activities, which function in a pathway for two-electron reduction of molecular oxygen, producing hydrogen peroxide and, subsequently, water. Activities of reduced NAD-oxidase and -peroxidase were inversely correlated with their sensitivities to oxygen. Bifidobacterium adolescentis exhibited lowered activities of these two enzymes; the activities were 10 to 20% of those observed with B. infantis, B. breve, and B. longum. These observations are compatible with the hypothesis that reduced NAD-oxidase and reduced NAD-peroxidase in Bifidobacterium species play a role in prevention of oxygen toxicity. Superoxide dismutase activity was also detected in Bifidobacterium species. Superoxide dismutase is probably not involved in detoxification of oxygen, because the activity of this enzyme was extremely low, and the sensitivity to oxygen varied independently of superoxide dismutase activity.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ISSN:0022-0302
1525-3198
DOI:10.3168/jds.S0022-0302(92)78105-3