Production of a novel bifunctional catalase-phenol oxidase of Scytalidium thermophilum in the presence of phenolic compounds

Çoruh, Nursen
Karakaş, Gürkan
A novel bifunctional catalase with additional phenol oxidase activity (CATPO) is produced by the thermophilic fungus, Scytalidium thermophilum, in a growth-associated manner. In order to study the biological significance of this dual enzyme in relation to phenolic compounds, 14 phenolics were tested for their effect on growth and CATPO production. It was determined that some phenolics exerted a negative effect on growth (catechol, coumaric acid, hydroquinone, kaempferol, myricetin), while others either did not influence growth in a negative manner or enhanced growth by a maximum of 50% increase in biomass (caffeic acid, chlorogenic acid, catechin, gallic acid, resorcinol, vanillic acid). Hydroquinone and myricetin showed an antifungal effect and enhanced CATPO production, while catechol, coumaric acid, and kaempferol decreased CATPO production and showed a toxic effect at higher doses. In general, phenolics acting in an antioxidant manner exhibited a reverse interrelation with CATPO production. These results suggest that the presence of antioxidant phenolic compounds has an effect on enhancing its antioxidant activity; enzyme is therefore no longer required.


Characterization and analysis of the antioxidant capacity of functional phenolics oxidized by Scytalidium thermophilum catalase phenol oxidase (CATPO)
Söyler, Ulviye Betül; Ögel, Zümrüt Begüm; Şensoy, İlkay; Department of Food Engineering (2012)
Scytalidium thermophilum is a termophilic fungus that effectively produces the extracellular enzyme catalase phenol oxidase (CATPO). The enzyme is distinct among catalases with its bifunctionality of oxidising phenolic compounds in the absence of H2O2. CATPO is capable of oxidizing catechol, chlorogenic acid, caffeic acid and catechin which are ortho –diphenolic compounds. Diphenolic compounds are known as strong antioxidants. Catalase is one of the important antioxidant enzymes. Therefore, in this thesis t...
Oxidation of phenolic compounds by the bifunctional catalase-phenol oxidase (CATPO) from Scytalidium thermophilum
Avci, Gulden Koclar; Çoruh, Nursen; Bolukbasi, Ufuk; Ogel, Zumrut B. (Springer Science and Business Media LLC, 2013-01-01)
The thermophilic fungus Scytalidium thermophilum produces a novel bifunctional catalase with an additional phenol oxidase activity (CATPO); however, its phenol oxidation spectrum is not known. Here, 14 phenolic compounds were selected as substrates, among which (+)-catechin, catechol, caffeic acid, and chlorogenic acid yielded distinct oxidation products examined by reversed-phase HPLC chromatography method. Characterization of the products by LC-ESI/MS and UV-vis spectroscopy suggests the formation of dime...
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 ...
Purification, characterization, crystallization and preliminary x-ray structure determination of scytalidium thermophilum bifunctional catalase and identification of its catechol oxidase activity
Sutay, Didem; Bakır, Ufuk; Department of Chemical Engineering (2007)
In this study, the aim was identification and classification of the enzyme having phenol oxidase activity produced by a thermophilic fungus, Scytalidium thermophilum. For this purpose, enzyme production, purification, biochemical characterization and structural analysis by X-ray crystallography studies have been performed. At the beginning of the research, this enzyme was considered as a phenol oxidase and analyzed accordingly. However, during purification, amino acid sequencing and structural studies, the ...
Production, properties and application to biocatalysis of a novel extracellular alkaline phenol oxidase from the thermophilic fungus Scytalidium thermophilum
Ögel, Zümrüt Begüm; Yuzugullu, Y.; Mete, S.; Bakir, U.; Kaptan, Y.; Sutay, D.; Demir, Ayhan Sıtkı (Springer Science and Business Media LLC, 2006-08-01)
Scytalidium thermophilum produces an extracellular phenol oxidase on glucose-containing medium. Certain phenolic acids, specifically gallic acid and tannic acid, induce the expression of the enzyme. Production at 45 degrees C in batch cultures is growth-associated and is enhanced in the presence of 160 mu M CuSO4.5 H2O and 3 mM gallic acid. The highest enzyme activity is observed at pH 7.5 and 65 degrees C, on catechol. When incubated for 1 h at pH 7 and pH 8, 95% and 86% of the activity is retained. Thermo...
Citation Formats
Y. YUZUGULLU, Z. B. Ogel, U. B. BOLUKBASI, N. Çoruh, and G. Karakaş, “Production of a novel bifunctional catalase-phenol oxidase of Scytalidium thermophilum in the presence of phenolic compounds,” TURKISH JOURNAL OF BIOLOGY, pp. 697–704, 2011, Accessed: 00, 2020. [Online]. Available: