title: Efficiency of new fungal cellulase systems in boosting enzymatic degradation of barley straw lignocellulose.
abstract: This study examined the cellulytic effects on steam-pretreated barley straw of cellulose-degrading enzyme systems from the five thermophilic fungi Chaetomium thermophilum, Thielavia terrestris, Thermoascus aurantiacus, Corynascus thermophilus, and Myceliophthora thermophila and from the mesophile Penicillum funiculosum. The catalytic glucose release was compared after treatments with each of the crude enzyme systems when added to a benchmark blend of a commercial cellulase product, Celluclast, derived from Trichoderma reesei and a beta-glucosidase, Novozym 188, from Aspergillus niger. The enzymatic treatments were evaluated in an experimental design template comprising a span of pH (3.5-6.5) and temperature (35-65 degrees C) reaction combinations. The addition to Celluclast + Novozym 188 of low dosages of the crude enzyme systems, corresponding to 10 wt % of the total enzyme protein load, increased the catalytic glucose yields significantly as compared to those obtained with the benchmark Celluclast + Novozyme 188 blend. A comparison of glucose yields obtained on steam-pretreated barley straw and microcrystalline cellulose, Avicel, indicated that the yield improvements were mainly due to the presence of highly active endoglucanase activity/activities in the experimental enzyme preparations. The data demonstrated the feasibility of boosting the widely studied T. reeseicellulase enzyme system with additional enzymatic activity to achieve faster lignocellulose degradation. We conclude that this supplementation strategy appears feasible as a first step in identifying truly promising fungal enzyme sources for fast development of improved, commercially viable, enzyme preparations for lignocellulose degradation.
authors.affiliation: Novozymes A/S, Krogshoejvej 36, Bagsvaerd, DK-2880 Denmark.
authors.forename: Lisa
authors.initials: L
authors.lastname: Rosgaard
authors.forename: Sven
authors.initials: S
authors.lastname: Pedersen
authors.forename: Joel R
authors.initials: JR
authors.lastname: Cherry
authors.forename: Paul
authors.initials: P
authors.lastname: Harris
authors.forename: Anne S
authors.initials: AS
authors.lastname: Meyer
mesh_terms: D001203:Ascomycota / Q000201:enzymology*; D002475:Cellobiose / Q000378:metabolism; D002480:Cellulase / Q000378:metabolism*; D002482:Cellulose / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003470:Culture Media; D005285:Fermentation; D005947:Glucose / Q000378:metabolism; D001467:Hordeum / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008031:Lignin / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism*; D018547:Plant Stems / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D003470:Culture Media; D009097:Multienzyme Complexes; C036909:lignocellulose; D002475:Cellobiose; D002482:Cellulose; D008031:Lignin; D002480:Cellulase; D005947:Glucose