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Crystallization and preliminary X-ray analysis of a cold-active endo-?-1,4-D-xylanase from glycoside hydrolase family 8.

ABSTRACT: Endo-?-1,4-D-xylanases are used in a multitude of industrial applications. Native crystals of a cold-adapted xylanase from glycoside hydrolase family 8 were obtained by the vapour-diffusion technique. The crystals belonged to space group I222, with unit-cell parameters a=46.6, b=110.8, c=150.2?Å at 100?K, and diffracted to 2.7?Å resolution at a synchrotron source. The asymmetric unit is likely to contain one molecule, with a VM of 2.07?Å3?Da(-1), corresponding to a solvent content of ?40%.

SUBMITTER: Schoepe J

PROVIDER: S-EPMC3079997 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of a cold-active endo-β-1,4-D-xylanase from glycoside hydrolase family 8.

Schoepe Jan J Pollet Annick A Verjans Priscilla P Delcour Jan A JA Strelkov Sergei V SV Courtin Christophe M CM

Acta crystallographica. Section F, Structural biology and crystallization communications 20101224 Pt 1

Endo-β-1,4-D-xylanases are used in a multitude of industrial applications. Native crystals of a cold-adapted xylanase from glycoside hydrolase family 8 were obtained by the vapour-diffusion technique. The crystals belonged to space group I222, with unit-cell parameters a=46.6, b=110.8, c=150.2 Å at 100 K, and diffracted to 2.7 Å resolution at a synchrotron source. The asymmetric unit is likely to contain one molecule, with a VM of 2.07 Å3 Da(-1), corresponding to a solvent content of ∼40%. ...[more]

PMID: 21206049

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Project description:As classified by the Carbohydrate-Active Enzymes (CAZy) database, enzymes in glycoside hydrolase (GH) family 10 (GH10) are all monospecific or bifunctional xylanases (except a tomatinase), and no endo-β-1,4-glucanase has been reported in the family. Here, we identified Arcticibacterium luteifluviistationis carboxymethyl cellulase (AlCMCase) as a GH10 endo-β-1,4-glucanase. AlCMCase originated from an Arctic marine bacterium, Arcticibacterium luteifluviistationis SM1504T It shows low identity (<35%) with other GH10 xylanases. The gene encoding AlCMCase was overexpressed in Escherichia coli Biochemical characterization showed that recombinant AlCMCase is a cold-adapted and salt-tolerant enzyme. AlCMCase hydrolyzes cello- and xylo-configured substrates via an endoaction mode. However, in comparison to its significant cellulase activity, the xylanase activity of AlCMCase is negligible. Correspondingly, AlCMCase has remarkable binding capacity for cello-oligosaccharides but no obvious binding capacity for xylo-oligosaccharides. AlCMCase and its homologs are grouped into a branch separate from other GH10 xylanases in a phylogenetic tree, and two homologs also displayed the same substrate specificity as AlCMCase. These results suggest that AlCMCase and its homologs form a novel subfamily of GH10 enzymes that have robust endo-β-1,4-glucanase activity. In addition, given the cold-adapted and salt-tolerant characters of AlCMCase, it may be a candidate biocatalyst under certain industrial conditions, such as low temperature or high salinity.IMPORTANCE Cellulase and xylanase have been widely used in the textile, pulp and paper, animal feed, and food-processing industries. Exploring novel cellulases and xylanases for biocatalysts continues to be a hot issue. Enzymes derived from the polar seas might have novel hydrolysis patterns, substrate specificities, or extremophilic properties that have great potential for both fundamental research and industrial applications. Here, we identified a novel cold-adapted and salt-tolerant endo-β-1,4-glucanase, AlCMCase, from an Arctic marine bacterium. It may be useful in certain industrial processes, such as under low temperature or high salinity. Moreover, AlCMCase is a bifunctional representative of glycoside hydrolase (GH) family 10 that preferentially hydrolyzes β-1,4-glucans. With its homologs, it represents a new subfamily in this family. Thus, this study sheds new light on the substrate specificity of GH10.

Dataset Information

Crystallization and preliminary X-ray analysis of a cold-active endo-?-1,4-D-xylanase from glycoside hydrolase family 8.

Publications

Crystallization and preliminary X-ray analysis of a cold-active endo-β-1,4-D-xylanase from glycoside hydrolase family 8.

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