Synchrotron radiation small angle scattering studies of thermal stability of xylanase XYNII from Trichoderma longibrachiatum

✍ Scribed by Maciej Kozak

• Book ID: 101722234
• Publisher: Wiley (John Wiley & Sons)
• Year: 2006
• Tongue: English
• Weight: 268 KB
• Volume: 83
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.20605

✦ Synopsis

Abstract

Xylanase XYNII from Trichoderma longibrachiatum is a small protein of the molecular weight 21 kDa, belonging to the family 11 of glycosyl hydrolases, which catalyses hydrolysis of xylan. This article reports thermal stability study of xylanase XYN II conformation in the temperature range 15–65°C by the small angle synchrotron radiation scattering. The study has been performed at different pH conditions: at pH 4.0 (below the physiological optimum of the enzyme activity) at pH 5.8 close to the optimum for enzymatic activity and at pH 8.0. The radius of gyration and the pair distance distribution function p(r) have been analyzed to characterize the changes of the enzyme conformation on heating. In the environment of the pH close to that of the optimum for the enzymatic activity, xylanase shows the greatest thermal stability and undergoes denaturation only above 55°C. In the acidic and basic environments, the enzyme stability is much lower and denaturation begins at 45°C. On the basis of the SAXS data, the shape of the xylanase molecule in solution in different temperatures has been reconstructed using ab initio method and program DAMMIN. The shape of the xylanase molecule at room temperature is similar to the right hand, which is typically observed for xylanase crystal structure. In higher temperatures (close to the enzyme activity optimum), the conformation of the right hand is loosened and half opened. © 2006 Wiley Periodicals, Inc. Biopolymers 83: 668–674, 2006

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