Structural basis of the properties of an industrially relevant thermophilic xylanase

✍ Scribed by Gillian W. Harris; Richard W. Pickersgill; Ian Connerton; Philippe Debeire; Jean-Pierre Touzel; Christelle Breton; Serge Pérez

• Publisher: John Wiley and Sons
• Year: 1997
• Tongue: English
• Weight: 206 KB
• Volume: 29
• Category: Article
• ISSN: 0887-3585
• DOI: 10.1002/(sici)1097-0134(199709)29:1<77::aid-prot6>3.0.co;2-c

✦ Synopsis

A thermophilic xylanase from Bacillus strain D3 suitable for use as a bleach booster in the paper pulping industry has been identified and characterized. The enzyme is suited to the high temperature and alkaline conditions needed for using xylanases in the pulp industry. The xylanase is stable at 60 degrees C and relatively stable at high temperatures, with a temperature optimum of 75 degrees C. The pH optimum is 6, but the enzyme is active over a broad pH range. The xylanase has been cloned and sequenced, and the crystal structure has been determined. The structure of Bacillus D3 xylanase reveals an unusual feature of surface aromatic residues, which form clusters or "sticky patches" between pairs of molecules. These "sticky patches" on the surface of the enzyme are responsible for the tendency of the protein to aggregate at high concentrations in the absence of reagents such as ethylene glycol. The formation of dimers and higher order polymers via these hydrophobic contacts may also contribute to the thermostability of this xylanase.