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Purification and properties of an endo-(1→4)-β-d-xylanase from irpex lacteus (Polyporus tulipiferae)

✍ Scribed by Christine Hoebler; Jean-Marc Brillouet

Publisher
Elsevier Science
Year
1984
Tongue
English
Weight
870 KB
Volume
128
Category
Article
ISSN
0008-6215

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✦ Synopsis

A xylanase from Driselase (a commercial enzyme preparation), obtained from the basidiomycetes Irpex lacteus (Polyporus tulipiferae), was purified -32fold by desalting on Sephadex G-25, ion-exchange chromatography on DEAE-Sepharose CL-6B and CM-Sepharose CLdB, hydrophobic-interaction chromatography on Phenyl-Sepharose CL-4B, gel filtration on Ultrogel AcA54, and affinity chromatography on Concanavalin A-Ultrogel. The enzyme is a glycoprotein that contains 23% of sugars, mainly as glucose. Its molecular weight is 38,000 and its p1 7.6-8.0. The enzyme exhibited maximal activity at pH 4.6-5.2 and at 6O", and was completely inactivated within 30 min at 70". The K,,, values for larch 4-0methylglucuronoxylan were 2.8 (suspension in water) and 1 mg/mL (solution in 20% methyl sulfoxide). The xylanase degraded larchwood xylan to xylose, xylobiose, and xylotriose, as neutral end-products.

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