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General Properties of Beta-Galactosidase of Xanthomonas campestris
1Eastern Regional Research Center, Agricultural Research, Science and Education Administration, U.S. Department of Agriculture, Philadelphia, Pennsylvania 19118.
Applied and Environmental Microbiology
|September 1, 1979
Abstract:
Partially purified beta-galactosidase of Xanthomonas campestris required 32 to 37 degrees 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.

