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)

Vol. 110 480-487

Subject Categories

Environmental Engineering

Biological Sciences

DOI

10.1016/j.biortech.2012.01.116

More information

Latest update

8/24/2018