General Properties of Beta-Galactosidase of Xanthomonas campestris-Reference-Cited by-同舟云学术

General Properties of Beta-Galactosidase of Xanthomonas campestris

Published:1979-09 Issue:3 Volume:38 Page:554-556
ISSN:0099-2240
Container-title:Applied and Environmental Microbiology
language:en
Short-container-title:Appl Environ Microbiol

Author:

Frank Joseph F.¹,Somkuti George A.¹

Affiliation:

1. Eastern Regional Research Center, Agricultural Research, Science and Education Administration, U.S. Department of Agriculture, Philadelphia, Pennsylvania 19118

Abstract

Partially purified β-galactosidase of Xanthomonas campestris required 32 to 37�C and pH 5.5 to 5.8 for optimum activity. The enzyme had low affinity for lactose hydrolysis ( K m = 22 mM) and was inhibited by thiol group reagents, ethylenediaminetetraacetic acid, galactose, and d -galactal.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Link

https://journals.asm.org/doi/pdf/10.1128/aem.38.3.554-556.1979

Reference16 articles.

1. Purification and properties of f8-galactosidase of Bacillus subtilis;Anema P. J.;Biochim. Biophys. Acta,1964

2. Disc electrophoresis. II. Method and application to human serum proteins;Davis B. J.;Ann. N. Y. Acad. Sci.,1974

3. The determination of enzyme inhibitor constants;Dixon M.;Biochem. J.,1953

4. Occurrence of glycoside hydrolases in plant pathogenic and related bacteria;Hayward A. C.;J. Appl. Bacteriol.,1977

5. Induction and general properties of fl-galactosidase and B3-galactoside permease in Pseudomonas BAL-31;Hidalgo C.;J. Bacteriol.,1977

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