Adsorption of [beta]-glucosidases in two commercial preparations onto pretreated biomass and lignin

Enzyme recycling is a method to reduce the production costs for advanced bioethanol by lowering the overall use of enzymes. Commercial cellulase preparations consist of many different enzymes that are important for efficient and complete cellulose (and hemicellulose) hydrolysis. This abundance of di...

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Bibliographic Details
Published in:Biotechnology for biofuels 2013-11, Vol.6 (1), p.165-165
Main Authors: Haven, Mai Østergaard, Jargensen, Henning
Format: Article
Language:English
Subjects:
Adsorption
Albumin
Aspergillus niger
Biomass
Biomass chemicals
Cellulase
Cellulose
Colleges & universities
Enzymes
Ethylene glycol
Experiments
Fermentation
Lignin
Lignocellulose
Molecular weight
Proteins
Recycling
Triticum aestivum
Wheat
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Summary:Enzyme recycling is a method to reduce the production costs for advanced bioethanol by lowering the overall use of enzymes. Commercial cellulase preparations consist of many different enzymes that are important for efficient and complete cellulose (and hemicellulose) hydrolysis. This abundance of different activities complicates enzyme recycling since the individual enzymes behave differently in the process. Previously, the general perception was that [beta]-glucosidases could easily be recycled via the liquid phase, as they have mostly been observed not to adsorb to pretreated biomass or only adsorb to a minor extent. The results from this study with Cellic[R] CTec2 revealed that the vast majority of the [beta]-glucosidase activity was lost from the liquid phase and was adsorbed to the residual biomass during hydrolysis and fermentation. Adsorption studies with [beta]-glucosidases in two commercial preparations (Novozym 188 and Cellic[R] CTec2) to substrates mimicking the components in pretreated wheat straw revealed that the Aspergillus niger [beta]-glucosidase in Novozym 188 did not adsorb significantly to any of the components in pretreated wheat straw, whereas the [beta]-glucosidase in Cellic[R] CTec2 adsorbed strongly to lignin. Contrary to the [beta]-glucosidases in Novozym 188, the [beta]-glucosidases in Cellic[R] CTec2 adsorb significantly to lignin. The lignin adsorption observed for Cellic[R] CTec2 is usually not a problem during hydrolysis and fermentation since most of the catalytic activity is retained. However, adsorption of [beta]-glucosidases to lignin may prove to be a problem when trying to recycle enzymes in the production of advanced bioethanol.
ISSN:1754-6834
1754-6834
DOI:10.1186/1754-6834-6-165