Article ID Journal Published Year Pages File Type
6491984 Journal of Biotechnology 2012 7 Pages PDF
Abstract
► Several variants between endoglucanase CelA and the binding module CBM3a were constructed. ► Attachment of the binding module enhanced activity, particularly against insoluble substrates. ► Constructs CelA-BC and CelA-CB with CBM3a attached at N- and C-termini of the catalytic domain, respectively were prepared. ► CelA-BC was more active than CelA-CB. ► The binding residues and the active site residues are more favorably oriented with respect to the substrate in CelA-BC.
Related Topics
Physical Sciences and Engineering Chemical Engineering Bioengineering
Authors
, , , , , ,