Oxidation of phenolic compounds by the bifunctional catalase-phenol oxidase (CATPO) from Scytalidium thermophilum


Avci G. K. , ÇORUH N. , Bolukbasi U. , Ogel Z. B.

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, cilt.97, ss.661-672, 2013 (SCI İndekslerine Giren Dergi) identifier identifier identifier

  • Cilt numarası: 97 Konu: 2
  • Basım Tarihi: 2013
  • Doi Numarası: 10.1007/s00253-012-3950-2
  • Dergi Adı: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • Sayfa Sayıları: ss.661-672

Özet

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 dimers of dehydrocatechin type B (hydrophilic) and type A (hydrophobic), as well as oligomers, namely, a trimer and tetramer from (+)-catechin, the formation of a dimer and oligomer of catechol, a dimer from caffeic acid with a caffeicin-like structure, as well as trimeric and tetrameric derivatives, and a single major product from chlorogenic acid suggested to be a dimer. Based on the results, CATPO oxidizes phenolic compounds ranging from simple phenols to polyphenols but all having an ortho-diphenolic structure in common. The enzyme also appears to have stereoselectivity due to the oxidation of (+)-catechin, but not that of epicatechin. It is suggested that CATPO may contribute to the antioxidant mechanism of the fungus and may be of value for future food and biotechnology applications where such a bifunctional activity would be desirable.