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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URI

https://hdl.handle.net/11511/58019

Journal

NEW BIOTECHNOLOGY

DOI

https://doi.org/10.1016/j.nbt.2009.06.370

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Graduate School of Natural and Applied Sciences, Article

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Purification, characterization, and identification of a novel bifunctional catalase-phenol oxidase from Scytalidium thermophilum Kocabas, Didem Sutay; Bakir, Ufuk; Phillips, Simon E. V.; McPherson, Michael J.; Ögel, Zümrüt Begüm (Springer Science and Business Media LLC, 2008-06-01) 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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Citation Formats

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.