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Applied and Environmental Microbiology, September 1998, p. 3533-3535, Vol. 64, No. 9
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Purification and Properties of Two Thermostable Alkaline Xylanases from an Alkaliphilic Bacillus sp.

Amare Gessesse*

Department of Biology, Addis Ababa University, Addis Ababa, Ethiopia

Received 8 January 1998/Accepted 14 July 1998

Two xylanases, designated XylA and XylB, were purified from the culture supernatant of the alkaliphilic Bacillus sp. strain AR-009. The molecular masses of the two enzymes were estimated to be 23 kDa (XylA) and 48 kDa (XylB) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The optimum pHs for activity were 9 for XylA and 9 to 10 for XylB. The temperature optima for the activity of XylA were 60°C at pH 9 and 70°C at pH 8. XylB was optimally active at 75°C at pH 9 and 70°C at pH 8. Both enzymes were stable in a broad pH range and showed good stability when incubated at 60 and 65°C in pH 8 and 9 buffers.

* Mailing address: Department of Biology, Addis Ababa University, P.O. Box 1176, Addis Ababa, Ethiopia. Fax: (2511) 552350 or 552112.

Applied and Environmental Microbiology, September 1998, p. 3533-3535, Vol. 64, No. 9
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Lyon, P.-F., Beffa, T., Fischer, J. L., Aragno, M. (2000). Xylanase activity and thermostratification during the thermogenic phase of industrial composting in aerated trenches. Waste Manag Res 18: 174-183 [Abstract]  


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