Lignin boosts the cellulase performance of a GH-61 enzyme from Sporotrichum thermophile
Journal article, 2012
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 beta-glucan, carboxymethyl cellulose, lichenan, wheat arabinoxylan and birchwood xylan showing optimal activity at pH 8 and 65 degrees 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, beta-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.
degradation
treated wheat straw
Cellulose hydrolysis
endoglucanase
trichoderma-reesei
Glycoside hydrolase family 61
growth
iv
glycoside hydrolase family
Spruce-derived material
expression
Hydrothermally
Sporotrichum thermophile
antioxidant activity
Author
M. Dimarogona
National Technical University of Athens (NTUA)
E. Topakas
National Technical University of Athens (NTUA)
Lisbeth Olsson
Chalmers, Chemical and Biological Engineering, Industrial biotechnology
Wallenberg Wood Science Center (WWSC)
P. Christakopoulos
National Technical University of Athens (NTUA)
Bioresource Technology
0960-8524 (ISSN) 1873-2976 (eISSN)
Vol. 110 480-487Subject Categories
Environmental Engineering
Biological Sciences
DOI
10.1016/j.biortech.2012.01.116