Cellulose 1,4-β-cellobiosidase (non-reducing end)

[1] Development of such organisms, such as Saccharomyces cerevisiae which is capable of secreting high levels of cellobiohydrolases, is already underway.

[2][3][4][5] This enzyme catalyses the hydrolysis of (1→4)-β-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.

CBH1 from yeast, for example, is composed of a carbohydrate binding site, a linker region and a catalytic domain.

Further purification to bring the ethanol purity to roughly 99.5% Some notable improvements have been made in this area as well.

[10] This is an important development in the sense that it makes large scale, industrial applications more feasible.

CBH1 Structure, generated using pymol
CBH1 zoomed in on the active site where cellulose is cleaved into cellobiose, generated using pymol.