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. 1994 Dec;60(12):4620–4623. doi: 10.1128/aem.60.12.4620-4623.1994

Purification and some properties of a xylanase from Aspergillus sydowii MG49.

M Ghosh 1, G Nanda 1
PMCID: PMC202033  PMID: 7811101

Abstract

Aspergillus sydowii MG49 produces a 30-kDa exosplitting xylobiohydrolase during growth on xylan. A specific chemical modification and substrate protection analysis of purified xylanase provided evidence that tryptophan and carboxy and amino groups are present at the catalytic site of this enzyme. Thermal inactivation of the xylanase occurs because of irreversible polymolecular aggregation, which is slower in the presence of glycerol.

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Selected References

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