Catalytic properties of the endoxylanase I from Thermoascus aurantiacus

• Endo-β-1,4-xylanase I previously purified from Thermoascus aurantiacus solid state culture was further characterized. The enzyme had a molecular weight of 33 kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and 31 kDa by gel filtration. Thin layer chromatography (TLC) analysis showed that endoxylanase liberates aldotetrauronic acid MeGlcAα-1,2-Xylβ-1,4-Xylβ-1,4-Xyl as the shortest acidic fragment from glucuronoxylan and an isomeric xylotriose (Xyl3) of the structure Xylβ1-3Xylβ1-4Xyl from rhodymenan. The enzyme performed ideally on O-acetyl-4-O-methylglucuronoxylan, liberating large amounts of short acetylated and non-acetylated fragments. Also, the enzyme was capable to hydrolyse arabinoxylan to arabinose (Arab), xylose (Xyl) and xylobiose (Xyl2). The enzyme degraded pNPX (4-nitrophenyl β-D-xylopyranoside) by a complex reaction pathway that involved both hydrolysis and glycosyl transfer reactions. The enzyme tolerates the replacement of β-xylopyranosyl units in several artificial substrates by β-glucopyranosyl, α-L-arabinopyranosyl and α-L-arabinofuranosyl units and was active on pNPC (4-nitrophenyl β-D-cellobioside), pNP-Arap (4-nitrophenyl α-L-arabinopyranoside) and pNPAraf (4-nitrophenyl α-L-arabinofuranoside). The enzyme also hydrolysed the 4-methylumbelliferyl glycosides of β-D-xylobiose and β-D-xylotriose at the agluconic linkage. The results suggested that the xylanase I from T. aurantiacus has catalytic properties similar to those belonging to family 10. Copyright © 2001 Elsevier Science B.V.

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