Identification of GH10 xylanases in strains 2 and Mz5 of Pseudobutyrivibrio xylanivorans

GRILLI, DIEGO; JAN KOPEčNÝ; JAKUB MRÁZEK; ROMANA MARIN?EK-LOGAR; SEBASTIÁN PAEZ LAMA; MIGUEL SOSA ESCUDERO; GRACIELA N. ARENAS

FOLIA MICROBIOLOGICA

SPRINGER

Lugar: Berlin; Año: 2014 vol. 59 p. 507 - 514

0015-5632

Abstract Genes encoding glycosyl hydrolase family 11(GH11) xylanases and xylanases have been identified fromPseudobutyrivibrio xylanivorans. In contrast, little is knownabout the diversity and distribution of the GH10 xylanase instrains of P. xylanivorans. Xylanase and associated activitiesof P. xylanivorans have been characterized in detail in the typestrain, Mz5. The aim of the present study was to identifyGH10 xylanase genes in strains 2 and Mz5 of P. xylanivorans.In addition, we evaluated degradation and utilization of xylanby P. xylanivorans 2 isolated from rumen of Creole goats.After a 12-h culture, P. xylanivorans 2 was able to utilize up to53 % of the total pentose content present in birchwood xylan(BWX) and to utilize up to 62 % of a ethanol-acetic acidsolublefraction prepared from BWX. This is the first reportdescribing the presence of GH10 xylanase-encoding genes inP. xylanivorans. Strain 2 and Mz5 contained xylanases whichwere related to GH10 xylanase of Butyrivibrio sp. Identifying