Purification and properties of Streptococcus lactis beta-galactosidase.

Journal of Bacteriology
G A McFetersP R Elliker

Abstract

beta-Galactosidase of Streptococcus lactis 7962 was partially purified, and its properties were studied. Enzyme from only this strain of numerous lactic streptococci tested was stable in cell exudates prepared by various means. Cell-free extracts of the 7962 strain were prepared by sonic treatment of washed cells previously grown in presence of lactose to fully induce enzyme synthesis. Protamine sulfate precipitation of the nucleic acids and ammonium sulfate precipitation of protein were used for partial purification of the enzyme. The resulting enzyme, when resuspended in cold (5 C) phosphate buffer, was extremely labile. However, ammonium sulfate in high concentrations (0.85 m) stabilized and stimulated beta-galactosidase activity. Sephadex G-200 gel filtration was used to achieve further purification and to monitor homogeneity of the enzyme. Separation of the beta-galactosidase in buffer at 5 C yielded an enzyme elution pattern showing two peaks of activity. However, addition of the enzyme solution in 0.85 m ammonium sulfate to the column equilibrated with the same salt concentration yielded only one peak of enzyme activity. The data suggested that the native enzyme was dissociating into active subunits which were stabilized...Continue Reading

References

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Citations

Jan 1, 1978·Folia Microbiologica·M V Rao, S M Dutta
Oct 17, 1998·Comparative Immunology, Microbiology and Infectious Diseases·G SahooV K Singh
Apr 1, 1970·Journal of Bacteriology·R P Erickson, E Steers
Jun 1, 1979·Applied and Environmental Microbiology·S A de Bales, F J Castillo
Oct 1, 1971·Journal of Bacteriology·G A McFetersP R Elliker
Jul 1, 1972·Applied Microbiology·L PremiP R Elliker
Oct 8, 1968·Biochimica Et Biophysica Acta·L Biermann, M D Glantz
Mar 1, 1973·Archives of Oral Biology·C E NordA A Lindberg

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