Mode of action of a minor xylanase from Thermoascus aurantiacus on polysaccharides and model substrates.
The mode of action of a minor xylanase on a variety of polysaccharides and model substrates was investigated. The enzyme was excreted by Thermoascus aurantiacus grown in solid state fermentation (SSF). The purified enzyme had a molecular mass of 33,000. Thin layer chromatography analysis showed that the endoxylanase liberated short fragments from polysaccharides. The enzyme hydrolysed aryl-beta-D-cellobioside and the chromogenic (fluorogenic) 4-methylumbelliferyl-beta-glycosides of xylobiose (MeUmbXyl2) and xylotriose (MeUmbXyl3) at the agluconic linkage. The results suggested that the endoxylanase belonged to family 10.
Kalogeris
E
E
Department of Chemical Engineering, National Technical University of Athens, 5 Iroon Polytechniou St., Zografou Campus, Athens 15 700, Greece.
Christakopoulos
P
P
Kekos
D
D
Macris
B J
BJ