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

Dimarogona, M; Topakas, E; Olsson, L; Christakopoulos, P

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	https://dspace.lib.ntua.gr/xmlui/handle/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