A modular xylanase from mesophilic Cellulomonas fimi contains the same cellulose-binding and thermostabilizing domains as xylanases from thermophilic bacteria

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Calcium binding by the N-terminal cellulose-binding domain from Cellulomonas fimi beta-1,4-glucanase CenC.

The interaction of the N-terminal cellulose-binding domain, CBDN1, from Cellulomonas fimi beta-1,4-glucanase CenC with calcium was investigated using NMR spectroscopy and calorimetry. CBDN1 binds a single calcium ion with an equilibrium association constant of approximately 10(5) M-1 at 35 degreesC and pH 6.0. Binding is exothermic (-42 +/- 2 kJ mol-1) under these conditions and is accompanied ...

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3-1,4-Glycanase from Cellulomonas fimi

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Molecular and biochemical characterization of two xylanase-encoding genes from Cellulomonas pachnodae.

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Enhancing the stability of xylanase from Cellulomonas fimi by cell-surface display on Escherichia coli.

AIMS The cell-surface display of Cex, which encodes xylanase and exoglucanase from Cellulomonas fimi, was constructed on Escherichia coli using PgsA as the anchor protein. Characterization of the cell-surface display of Cex was performed. METHODS AND RESULTS PgsA was fused to the N-terminus of Cex and six histidines were utilized as spacers between the targeting and anchor proteins. Successfu...

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ژورنال

عنوان ژورنال: FEMS Microbiology Letters

سال: 1996

ISSN: 0378-1097

DOI: 10.1016/0378-1097(96)00101-2