Authors
Fernando Segato, André RL Damasio, Thiago Augusto Gonçalves, Mario T Murakami, Fabio M Squina, MariadeLourdesTM Polizeli, Andrew J Mort, Rolf A Prade
Publication date
2012/12
Journal
Biotechnology for biofuels
Volume
5
Issue
1
Pages
21
Publisher
BioMed Central
Description
Background
Cellulose consisting of arrays of linear beta-1,4 linked glucans, is the most abundant carbon-containing polymer present in biomass. Recalcitrance of crystalline cellulose towards enzymatic degradation is widely reported and is the result of intra- and inter-molecular hydrogen bonds within and among the linear glucans. Cellobiohydrolases are enzymes that attack crystalline cellulose. Here we report on two forms of glycosyl hydrolase family 7 cellobiohydrolases common to all Aspergillii that attack Avicel, cotton cellulose and other forms of crystalline cellulose.
Results
Cellobiohydrolases Cbh1 and CelD have similar catalytic domains but only Cbh1 contains a carbohydrate-binding domain (CBD) that binds to cellulose. Structural superpositioning of Cbh1 and CelD on the Talaromyces emersonii Cel7A 3-dimensional structure, identifies the …
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