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Purification, characterization and identification of a novel bifunctional catalase-phenol oxidase from Scytalidium thermophilum
Date
2009-09-01
Author
Kocabas, D. Sutay
Bakir, U.
Phillips, S. E.
Mcpherson, M. J.
Ögel, Zümrüt Begüm
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Cite This
URI
https://hdl.handle.net/11511/58019
Journal
NEW BIOTECHNOLOGY
DOI
https://doi.org/10.1016/j.nbt.2009.06.370
Collections
Graduate School of Natural and Applied Sciences, Article
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A novel bifunctional catalase with an additional phenol oxidase activity was isolated from a thermophilic fungus, Scytalidium thermophilum. This extracellular enzyme was purified ca. 10-fold with 46% yield and was biochemically characterized. The enzyme contains heme and has a molecular weight of 320 kDa with four 80 kDa subunits and an isoelectric point of 5.0. Catalase and phenol oxidase activities were most stable at pH 7.0. The activation energies of catalase and phenol oxidase activities of the enzyme ...
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D. S. Kocabas, U. Bakir, S. E. Phillips, M. J. Mcpherson, and Z. B. Ögel, “Purification, characterization and identification of a novel bifunctional catalase-phenol oxidase from Scytalidium thermophilum,”
NEW BIOTECHNOLOGY
, pp. 0–0, 2009, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/58019.