Purification and some properties of a xylanase from Aspergillus sydowii MG49

Author:

Ghosh M1,Nanda G1

Affiliation:

1. Department of Microbiology, Bose Institute, Calcutta, India.

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.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Reference6 articles.

1. Essential carboxy groups in xylanase A;Bray M. R.;Biochem. J.,1990

2. Capalash N. P. Sharma and K. G. Gupta. 1990. Use of a modified cupric acetate method for the detection and quantitation of xylanolytic activities: a comparative study with the Congo red

3. Dominiguez J. M. C. Acebal J. Jimenez method. Lett. Appl. Microbiol. 10:151-154.

4. Aspergillus sydowii MG49 is a strong producer of thermostable xylanolytic enzymes;Ghosh M.;Enzyme Microb. Technol.,1993

5. Ghosh M. and G. Nanda. 1993. Thermostability of 3-xylosidase

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