Neurospora crassa 870 produced 14 and 0.025 U of extracellular xylanase (1,4-β-d-xylan xylanohydrolase; EC 22.214.171.124) and β-xylosidase (1,4-β-xylan xylohydrolase; EC 126.96.36.199) per ml, respectively, in 4 days when commercial xylan was used as a carbon source. The effects of pH and carbon sources on xylanase production by N. crassa are discussed. Two xylanases (I and II) were purified and had pI values of 4.8 and 4.5 and molecular weights of 33,000 and 30,000. The maximum degree of hydrolysis of xylan by the extracellular culture broth was 66% in 4 h. The end products of xylan hydrolysis by xylanase I and II showed the presence of xylose, xylobiose, xylotriose, xylotetraose, xylopentose, and arabinose, indicating that they are endoxylanases capable of hydrolyzing 1,3-α-l-arabinofuranosyl branch points. Both xylanases showed activity toward carboxymethyl cellulose but no activity toward para-nitrophenyl-β-d-xyloside or laminarin. Xylanase I showed appreciable activity toward para-nitrophenyl-β-d-glucoside, whereas xylanase II was inactive
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