title: General Properties of Beta-Galactosidase of Xanthomonas campestris.
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.
authors.affiliation: Eastern Regional Research Center, Agricultural Research, Science and Education Administration, U.S. Department of Agriculture, Philadelphia, Pennsylvania 19118.
authors.forename: J F
authors.initials: JF
authors.lastname: Frank
authors.forename: G A
authors.initials: GA
authors.lastname: Somkuti