Abstract
An endo-1,4-β-xylanase (EC 3.2.1.8) was isolated from the culture medium of Cryptococcus albidus. The enzyme was glycosylated and had an apparent molecular weight of 48 000. The enzyme preparation was resolved by isoelectric focusing into two xylanase components with p I values of 5.7 and 5.3, respectively. In time course digestion the enzyme degraded xylan, producing first a mixture of xylose oligosaccharides of various lengths and mainly xylose and xylobiose as end-products. The amino acid sequence of the first 72 residues shows some homology with the regions surrounding the catalytic residues Glu-35 and Asp-52 of egg lysozyme. The homology suggests a lysozyme-type mechanism of glycosidic bond cleavage for xylanase.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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