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Purification and some properties of a xylanase from Aspergillus sydowii MG49
Applied and Environmental Microbiology
|December 1, 1994
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.
Insights
Aspergillus sydowii MG49 produces a xylobiohydrolase enzyme that breaks down xylan. Chemical analysis identified key amino acid groups within the enzyme's active site, crucial for its function.
Area of Science:
- Biochemistry
- Enzymology
- Microbiology
Background:
- Xylanases are crucial enzymes for biomass degradation.
- Aspergillus sydowii is a fungal species known to produce various enzymes.
Purpose of the Study:
- To characterize the 30-kDa exosplitting xylobiohydrolase produced by Aspergillus sydowii MG49.
- To investigate the catalytic site and thermal stability of the purified xylanase.
Main Methods:
- Enzyme purification from Aspergillus sydowii MG49.
- Chemical modification of the purified xylanase.
- Substrate protection analysis.
- Thermal inactivation studies.
Main Results:
- A 30-kDa xylobiohydrolase was produced by Aspergillus sydowii MG49 on xylan.
- Chemical modification and substrate protection revealed tryptophan, carboxy, and amino groups at the enzyme's catalytic site.
- The xylanase undergoes thermal inactivation via irreversible polymolecular aggregation.
- Glycerol addition significantly slowed the rate of thermal inactivation.
Conclusions:
- The catalytic site of the Aspergillus sydowii MG49 xylanase contains essential tryptophan and charged amino acid groups.
- The enzyme's thermal stability is limited by aggregation, which can be mitigated by cryoprotectants like glycerol.