Degradation of phenolic compounds by the yeast Candida tropicalis HP 15. II. Some properties of the first two enzymes of the degradation pathway
- 10 January 1986
- journal article
- research article
- Published by Wiley in Journal of Basic Microbiology
- Vol. 26 (5) , 271-281
- https://doi.org/10.1002/jobm.3620260505
Abstract
The first two enzymes of the phenol degradation pathway were determined and characterized in crude extracts from Candida tropicalis HP 15. The phenol hydroxylase (EC 1.14.13.7) was a stable NADPH2‐ and FAD‐dependent enzyme with a pH‐optimum of 7.6 to 8.0 and a broad substrate specificity. Influence of ultrasound rapidly reduced the enzyme activity. The catechol 1,2‐oxygenase (EC 1.13.1.1) had a broad pH‐optimum between 7.5 and 9.6 and a limited substrate specificity. Two active protein bands indicating the presence of two isofunctional enzymes were detectable after electrophoretic separation of crude and partially purified extracts on polycrylamide gels and specific staining for catechol 1,2‐oxygenase activity.This publication has 23 references indexed in Scilit:
- Degradation of phenolic compounds by the yeast Candida tropicalis HP 15 I. Physiology of growth and substrate utilizationJournal of Basic Microbiology, 1985
- Rapid reaction studies on the oxygenation reactions of catechol dioxygenase.Journal of Biological Chemistry, 1983
- Degradation of catechol, methylcatechols and chlorocatechols byPseudomonassp. HV3FEMS Microbiology Letters, 1983
- Degradation of phenol by Streptomyces setoniiCanadian Journal of Microbiology, 1983
- The Purification and Properties of 2,4‐Dichlorophenol Hydroxylase from a Strain of Acinetobacter SpeciesEuropean Journal of Biochemistry, 1982
- Phenol Hydroxylase from YeastEuropean Journal of Biochemistry, 1975
- Phenol Hydroxylase from YeastEuropean Journal of Biochemistry, 1973
- Purification and Properties of Catechol 1,2‐Oxygenase from Trichosporon cutaneumEuropean Journal of Biochemistry, 1970
- Phenol hydroxylaseBiochimica et Biophysica Acta, 1962
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951