Structural and biochemical analyses of glycoside hydrolase families 5 and 26 β-(1,4)-mannanases from Podospora anserina reveal differences upon manno-oligosaccharide catalysis.

@article{Couturier2013StructuralAB,
  title={Structural and biochemical analyses of glycoside hydrolase families 5 and 26 β-(1,4)-mannanases from Podospora anserina reveal differences upon manno-oligosaccharide catalysis.},
  author={Marie Couturier and Alain Roussel and Anna L Rosengren and P. Leone and Henrik St{\aa}lbrand and Jean-Guy Berrin},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 20},
  pages={14624-35}
}
The microbial deconstruction of the plant cell wall is a key biological process that is of increasing importance with the development of a sustainable biofuel industry. The glycoside hydrolase families GH5 (PaMan5A) and GH26 (PaMan26A) endo-β-1,4-mannanases from the coprophilic ascomycete Podospora anserina contribute to the enzymatic degradation of lignocellulosic biomass. In this study, P. anserina mannanases were further subjected to detailed comparative analysis of their substrate… CONTINUE READING
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