Abstract
A xylanase from Driselase (a commercial enzyme preparation), obtained from the basidiomycetes Irpex lacteus (Polyporus tulipiferae), was purified ∼32-fold by desalting on Sephadex G-25, ion-exchange chromatography on DEAE-Sepharose CL-6B and CM-Sepharose CL-6B, 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 pI 7.6–8.0. The enzyme exhibited maximal activity at pH 4.6–5.2 and at 60°, and was completely inactivated within 30 min at 70°. The K m values for larch 4- O-methylglucuronoxylan 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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