Purification and characterization of a β-galactosidase from Treponema phagedenis (Reiter strain)

A beta -galactosidase was highly purified from a cellular extract of Treponema phagedenis (Reiter strain) by ammonium sulfate precipitation and successive chromatography on Sepharose 6B and DEAE-Sephadex. The purified enzyme was 580,000. The optimal pH, ionic strength, and temperature were 6.5, 0.1,...

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Bibliographic Details
Published in:Current microbiology 1983-01, Vol.8 (6), p.341-345
Main Authors: TAKAHASHI, T, SUGAHARA, T, YAMAYA, S.-I
Format: Article
Language:English
Subjects:
Bacteriology
beta -D-galactosidase
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Metabolism. Enzymes
Microbiology
Treponema phagedenis
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Summary:A beta -galactosidase was highly purified from a cellular extract of Treponema phagedenis (Reiter strain) by ammonium sulfate precipitation and successive chromatography on Sepharose 6B and DEAE-Sephadex. The purified enzyme was 580,000. The optimal pH, ionic strength, and temperature were 6.5, 0.1, and 50 degree C, respectively. The enzyme was stable only at around pH 6.5 and at temperatures lower than 35 degree C.
ISSN:0343-8651
1432-0991
DOI:10.1007/BF01573706