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. 1979 Sep;38(3):554–556. doi: 10.1128/aem.38.3.554-556.1979

General Properties of Beta-Galactosidase of Xanthomonas campestris

Joseph F Frank 1, George A Somkuti 1
PMCID: PMC243532  PMID: 16345439

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 (Km = 22 mM) and was inhibited by thiol group reagents, ethylenediaminetetraacetic acid, galactose, and d-galactal.

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Selected References

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