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Xylan oligosaccharides and cellobiohydrolase I ( Tr Cel7A) interaction and effect on activity by Martin J Baumann; Kim Borch; Peter Westh is a Engineering article available to read on EtoBox.

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## Background The well-studied cellulase mixture secreted by __Trichoderma reesei__ (anamorph to __Hypocrea jecorina__) contains two cellobiohydolases (CBHs), cellobiohydrolase I (__Tr__Cel7A) and cellobiohydrolase II (__Tr__CeI6A), that are core enzymes for the solubilisation of cellulose. This has attracted significant research interest because of the role of the CBHs in the conversion of biomass to fermentable sugars. However, the CHBs are notoriously slow and susceptible to inhibition, which presents a challenge for the commercial utilisation of biomass. The xylans and xylan fragments that are also present in the biomass have been suggested repeatedly as one cause of the reduced activity of CHBs. Yet, the extent and mechanisms of this inhibition remain poorly elucidated. Therefore, we studied xylan oligosaccharides (XOSs) of variable lengths with respect to their binding and inhibition of both __Tr__Cel7A and an enzyme variant without the cellulose-binding domain (CBM). ## Results We studied the binding of XOSs to __Tr__Cel7A by isothermal titration calorimetry. We found that XOSs bind to __Tr__Cel7A and that the affinity increases commensurate with XOS length. The CBM, on the

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Author

Martin J Baumann; Kim Borch; Peter Westh

Publisher

BioMed Central; Springer (Biomed Central Ltd.); [London]: BioMed Central; Springer Science and Business Media LLC (ISSN 1754-6834)

Published

2011

Language

EN

Field

Engineering (Physical Sciences)