Action of xylan deacetylating enzymes on monoacetyl derivatives of 4-nitrophenyl glycosides of β-D-xylopyranose and α-l-arabinofuranose

Peter Biely, Mária Mastihubová, Maija Tenkanen, Jaime Eyzaguirre, Xin Liang Li, Mária Vršanská

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

39 Citas (Scopus)

Resumen

Measurements of esterase activity by enzyme-coupled assays on monoacetates of 4-nitrophenyl β-D-xylopyranoside and 4-nitrophenyl α-l-arabinofuranoside showed that acetylxylan esterases of families 1, 4 and 5 produced by Trichoderma reesei and Penicillium purpurogenum have a strong preference for deacetylation of position 2 in xylopyranosides. The acetylxylan esterases exhibit only weak activity on acetylated arabinofuranosides, with 2-acetate as the best substrate. Acetyl esterases of family 16 produced by the same two fungi deacetylate in xylopyranosides preferentially positions 3 and 4. Their specific activity on arabinofuranosides is also much lower than on xylopyranosides, however, substantially greater than that in the case of typical acetylxylan esterases.

Idioma originalInglés
Páginas (desde-hasta)137-142
Número de páginas6
PublicaciónJournal of Biotechnology
Volumen151
N.º1
DOI
EstadoPublicada - 10 ene 2011

Áreas temáticas de ASJC Scopus

  • Biotecnología
  • Bioingeniería
  • Microbiología y biotecnología aplicadas

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Profundice en los temas de investigación de 'Action of xylan deacetylating enzymes on monoacetyl derivatives of 4-nitrophenyl glycosides of β-D-xylopyranose and α-l-arabinofuranose'. En conjunto forman una huella única.

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