TECHNOLOGY FOCUS - BIOTECHNOLOGY - Preferred Xylanase: The xylanase is obtainable from a strain belonging to the genus Bacillus, preferably from a strain of B. halodurans. It is obtainable from B. halodurans S7. The xylanase produced by B. halodurans S7 is deposited at Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH on 2005-03-14 under the accession number: DSM 17179. The xylanase has the nucleotide sequence as AY687345. The xylanase has over 80 % peak activity at pH 6-10.5, preferably pH 8-10.5, and at temperatures of 65-82degreesC. It has full activity for 12 hours from pH 5.5-10.5 at 50degreesC. The xylanase is also optimally active at 75degreesC and 70degreesC at pH 9 and 10, respectively. The xylanase is inactive regarding the substrates CMC, avicel, laminarin, p-nitrophenyl (pNP)-beta-galactopyranoside, pNP-alpha-glucopyranoside, pNP-beta-xylopyranoside, pNP-alpha-L-arabinofuranoside, pNP-acetate, or pNP-alpha-D-xylopyranoside. The xylanase is free of binding domains to avicel or xylan. The xylanase is sensitive to Mn2+-ions, and is insensitive to Hg2+-ions. The xylanase is also insensitive to EDTA. EXAMPLE - Cells were removed by centrifugation from a 36 hour old culture and the liquid supernatant was used as the enzyme source. The protein was precipitated from the cell-free culture supernatant by adding solid ammonium sulfate to 60% saturation. The pellet was recovered by centrifugation, dissolved in minimal amount of water and dialyzed against deionized water with three changes. Finally, the enzyme solution was equilibrated with 50 mM Tris-HCl buffer, pH 8.0. The dialysate was centrifuged and undissolved material was removed. The clear supernatant was put on DEAE Sepharose fast flow column equilibrated with the same buffer. Elution was performed with a linear gradient of 0-0.5 M NaCl. Fractions exhibiting xylanolytic activity were pooled and concentrated. The concentrate was fractionated using Sephadex G-75 column at a flow Fate of 10 ml/h. Xylanolytic fractions were pooled, concentrated and refractionated on the same G-75 column at a flow rate of 5 ml/h. The enzyme obtained after the second gel filtration was used for characterization.