The primary structure of xylanase from Thermoascus aurantiacus

The amino acid sequence of xylanase isolated from the culture medium of Thermoascus aurantiacus was determined. It had 269 amino acid residues with an alpha-N-acetyl group at the amino terminus. The structure of blocked N-terminal 11 amino acid tryptic peptide except for acetylalanine was determined by sequence analysis of peptides derived from partial acid hydrolysis and from thermolysin digestion. The blocked N-terminal amino acid was determined as N-acetylalanine by electron ionization mass spectrometry. The sequence comparison of xylanase from T. aurantiacus with the xylanases of alkalophilic Bacillus sp C-125 and Cryptococcus albidus showed 40% similarity. Xylanase from T. aurantiacus had up to 15% similarity with the other two xylanases known. All the five xylanases showed a higher degree of similarity at the level of secondary structure.