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Lignin boosts the cellulase performance of a GH-61 enzyme from Sporotrichum thermophile

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dc.contributor.author Dimarogona, M en
dc.contributor.author Topakas, E en
dc.contributor.author Olsson, L en
dc.contributor.author Christakopoulos, P en
dc.date.accessioned 2014-03-01T02:09:29Z
dc.date.available 2014-03-01T02:09:29Z
dc.date.issued 2012 en
dc.identifier.issn 09608524 en
dc.identifier.uri http://hdl.handle.net/123456789/29853
dc.subject Cellulose hydrolysis en
dc.subject Glycoside hydrolase family 61 en
dc.subject Hydrothermally treated wheat straw en
dc.subject Sporotrichum thermophile en
dc.subject Spruce-derived material en
dc.subject.other Alcohol oxidase en
dc.subject.other Carboxy-methyl cellulose en
dc.subject.other Cellulose hydrolysis en
dc.subject.other Enhancing capacity en
dc.subject.other Glycoside hydrolase family 61 en
dc.subject.other Glycoside hydrolases en
dc.subject.other Hydrothermally treated en
dc.subject.other Lignin contents en
dc.subject.other Ligno-cellulosics en
dc.subject.other Methylotrophic yeasts en
dc.subject.other Optimal activity en
dc.subject.other Pichia Pastoris en
dc.subject.other Radical scavenging en
dc.subject.other Reducing substances en
dc.subject.other Reductants en
dc.subject.other Sporotrichum thermophile en
dc.subject.other Synergistic activity en
dc.subject.other Thermophilic fungus en
dc.subject.other Transcriptional control en
dc.subject.other Wheat arabinoxylan en
dc.subject.other Cellulose en
dc.subject.other Ethanol en
dc.subject.other Hydrolysis en
dc.subject.other Lignin en
dc.subject.other Yeast en
dc.subject.other Enzymes en
dc.subject.other alcohol oxidase en
dc.subject.other arabinoxylan en
dc.subject.other beta glucan en
dc.subject.other carboxymethylcellulose en
dc.subject.other cellulase en
dc.subject.other lignin en
dc.subject.other xylan en
dc.subject.other barley en
dc.subject.other enzyme activity en
dc.subject.other fungus en
dc.subject.other guideline en
dc.subject.other lichen en
dc.subject.other lignin en
dc.subject.other performance assessment en
dc.subject.other pH en
dc.subject.other scavenging (chemistry) en
dc.subject.other substrate en
dc.subject.other wheat en
dc.subject.other article en
dc.subject.other controlled study en
dc.subject.other fungus en
dc.subject.other gene expression en
dc.subject.other hydrolysis en
dc.subject.other nonhuman en
dc.subject.other pH en
dc.subject.other Pichia pastoris en
dc.subject.other priority journal en
dc.subject.other saccharification en
dc.subject.other sporotrichum thermophile en
dc.subject.other Alcohol Oxidoreductases en
dc.subject.other Base Sequence en
dc.subject.other Cellulase en
dc.subject.other DNA Primers en
dc.subject.other Hot Temperature en
dc.subject.other Hydrogen-Ion Concentration en
dc.subject.other Hydrolysis en
dc.subject.other Lignin en
dc.subject.other Pichia en
dc.subject.other Polymerase Chain Reaction en
dc.subject.other Promoter Regions, Genetic en
dc.subject.other Sporothrix en
dc.subject.other Substrate Specificity en
dc.subject.other Corynascus heterothallicus en
dc.subject.other Fungi en
dc.subject.other Hordeum en
dc.subject.other Picea en
dc.subject.other Pichia pastoris en
dc.subject.other Triticum aestivum en
dc.title Lignin boosts the cellulase performance of a GH-61 enzyme from Sporotrichum thermophile en
heal.type journalArticle en
heal.identifier.primary 10.1016/j.biortech.2012.01.116 en
heal.identifier.secondary http://dx.doi.org/10.1016/j.biortech.2012.01.116 en
heal.publicationDate 2012 en
heal.abstract An enzyme belonging to the glycoside hydrolase family 61 from the thermophilic fungus Sporotrichum thermophile, was functionally expressed in the methylotrophic yeast Pichia pastoris under the transcriptional control of the alcohol oxidase (AOX1) promoter. The enzyme hydrolyzed barley β-glucan, carboxymethyl cellulose, lichenan, wheat arabinoxylan and birchwood xylan showing optimal activity at pH 8 and 65. °C. A 2:1 mixture of Celluclast 1.5. L and StCel61a was capable of increasing the degree of spruce conversion by 42%. The use of substrates with varying lignin content permitted the detection of a dependence of the enhancing capacity of StCel61a on the radical scavenging capacity of the different lignocellulosics. In the presence of a reductant, StCel61a boosted the efficiency of a mixture of purified cellulases (EGII, CBHI, β-GLUC) by 20%. The synergistic activity exhibited by StCel61a and its dependence on reducing substances provide guidelines for process design towards the production of economically viable bioethanol. © 2012 Elsevier Ltd. en
heal.journalName Bioresource Technology en
dc.identifier.doi 10.1016/j.biortech.2012.01.116 en
dc.identifier.volume 110 en
dc.identifier.spage 480 en
dc.identifier.epage 487 en


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