Abstract
The extracellular xylanase from Bacillus stearothermophilus T-6 is a thermostable alkaline tolerant enzyme that was found to bleach pulp optimally at pH 9 and 65°C, and was successfully used in a large-scale biobleaching mill trial. In an attempt to obtain a heavy atom derivative suitable for complete X-ray analysis, xylanase T-6 was labeled biosynthetically with seleno-methionine, resulting in a 'built-in' array of atoms with specific X- ray anomalous scattering signal. Optimization of growth conditions resulted in over 0.8 g of homogenous seleno-methionine xylanase T-6 per liter culture. The seleno-methionine enzyme was shown to be fully active and produced single crystals suitable for complete multiple wavelength anomalous diffraction (MAD) structural analysis. (C) 2000 Elsevier Science B.V.
| Original language | English |
|---|---|
| Pages (from-to) | 83-86 |
| Number of pages | 4 |
| Journal | Journal of Biotechnology |
| Volume | 78 |
| Issue number | 1 |
| DOIs | |
| State | Published - 29 Feb 2000 |
Bibliographical note
Funding Information:This study was supported by grants from the Israeli Ministry of Science and the Arts, Israel (No. 5932 and No. 4935), (to YS, TB and GS) and grants from the United States-Israel Binational Science Foundation (BSF), Jerusalem, Israel (No. 93-171 and 96-178) (to YS). Support was also provided by the Otto Meyerhof Center for Biotechnology established by the Minerva Foundation, Germany. AT was supported by the Otto Schwartz fellowship of the Hebrew University. VB was supported by the Center of Absorption in Science, Ministry of Immigration absorption and the Ministry of Science and Arts, State of Israel (Gilady Program). We thank Emily Parker and Chris Abell (Department of Chemistry, Cambridge) for the mass determinations.
Keywords
- Bacillus stearothermophilus
- Overproduction
- Seleno-methionine
- Structure-function
- X- ray
- Xylanase