Production, purification and characterization of Scytalidium thermophilum phenol oxidases

Sutay, D
Bakir, U
Ögel, Zümrüt Begüm


Investigation of thin semiconductor coatings and their antibacterial properties
Erkan, A; Bakir, U; Karakaş, Gürkan (2005-08-01)
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...
Production of recombinant human erythropoietin from Pichia pastoris and its structural analysis
Celik, E.; Çalık, Pınar; Halloran, S. M.; Oliver, S. G. (Wiley, 2007-12-01)
Aims: To design and investigate a recombinant expression system producing a therapeutically important glycoprotein, human erythropoietin (rHuEPO), by Pichia pastoris.
Preparation of cross-linked tyrosinase aggregates
Aytar, Burcu Selin; Bakir, Ufuk (Elsevier BV, 2008-02-01)
Tyrosinase from mushroom was immobilized as a cross-linked enzyme aggregate (CLEA) via precipitation with ammonium sulfate and cross-linking with glutaraldehyde. The effects of precipitation and cross-linking on CLEA activity were investigated and the immobilized tyrosinase was characterized. Sixty percent ammonium sulfate saturation and 2% glutaraldehyde were used; a 3-h cross-linking reaction at room temperature, at pH 7.0 was performed; particle sizes of the aggregates were reduced; consequently, 100% ac...
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 ...
Citation Formats
D. Sutay, U. Bakir, and Z. B. Ögel, “Production, purification and characterization of Scytalidium thermophilum phenol oxidases,” 2005, vol. 118, Accessed: 00, 2020. [Online]. Available: