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Appl Environ Microbiol. 1965 September; 13(5): 686-693
Copyright © 1965 American Society for Microbiology. All Rights Reserved.

Effect of Culture Conditions on the Production of D-Galactose Oxidase by Dactylium dendroides1

Z. Markus, G. Miller2 and G. Avigad

Department of Biological Chemistry, The Hebrew University, Jerusalem, Israel

ABSTRACT

The effects on enzyme production of inoculum size and age, medium composition, and culture conditions were studied in shake flasks and in a pilot-plant fermentor. Using a medium consisting of glucose, yeast extract, and inorganic salts in deionized water, we found that the addition of Cu++ was essential for the formation of active enzyme. Cultures grown in the absence of added copper produced an inactive enzyme protein which could be activated by 10-3 M Cu++. Thiamine fulfilled all requirements for exogenous vitamins for growth and enzyme production. Glucose concentrations higher than 1% markedly suppressed enzyme formation. The mycelium inactivated the enzyme on prolonged incubation of the culture. Mycelial autolysates and sonic extracts were found to contain a thermostable and slowly dialyzable galactose oxidase-inactivating factor. The experiments suggest that this factor operates as a chelating agent which forms complexes with the copper of the enzyme. Copper ions (10-3 M) prevented enzyme inactivation and restored activity to samples previously inactivated by this factor.

FOOTNOTES

2 Permanent address: Israel Institute for Biological Research, Ness-Ziona, Israel.

1 Taken in part from a Ph.D. Thesis to be submitted to the Hebrew University by Z. Markus.

Appl Environ Microbiol. 1965 September; 13(5): 686-693
Copyright © 1965 American Society for Microbiology. All Rights Reserved.





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