Thermostability is an important property of xylanase because high temperature is required for its applications, such as wood pulp bleaching, baking, and animal feedstuff processing. In this study, from , a moderately thermophilic gram-negative bacterium, was modified via site-directed mutagenesis (based on its 3D structure) to obtain thermostable xylanase, and the properties of this enzyme were analyzed. Results revealed that the half-life of xylanase at 65°C increased from 10 to 50 min after a disulfide bridge was introduced between the α-helix and its adjacent β-sheet at S98 and N145. Further mutation at the side of A153E named XynB-CE in the C-terminal of this α-helix enhanced the half-life of xylanase for 60 min at 65°C. Therefore, the mutant may be utilized for industrial applications.
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http://dx.doi.org/10.4014/jmb.1705.05026 | DOI Listing |
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