scholarly journals Characterization of a Neocallimastix patriciarum cellulase cDNA (celA) homologous to Trichoderma reesei cellobiohydrolase II.

1996 ◽  
Vol 62 (6) ◽  
pp. 1889-1896 ◽  
Author(s):  
S Denman ◽  
G P Xue ◽  
B Patel
Keyword(s):  
Trichoderma Reesei ◽  
Neocallimastix Patriciarum ◽  
Cellobiohydrolase Ii

Efficient secretion of Trichoderma reesei cellobiohydrolase II in Schizosaccharomyces pombe and characterization of its products

1998 ◽  
Vol 49 (3) ◽  
pp. 301-308 ◽  
Author(s):  
H. Okada ◽  
T. Sekiya ◽  
K. Yokoyama ◽  
H. Tohda ◽  
H. Kumagai ◽  
...  
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Trichoderma Reesei ◽  
Cellobiohydrolase Ii

scholarly journals Electrophysiological characterization of a diverse group of sugar transporters from Trichoderma reesei

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Sami Havukainen ◽  
Jonai Pujol-Giménez ◽  
Mari Valkonen ◽  
Ann Westerholm-Parvinen ◽  
Matthias A. Hediger ◽  
...  
Keyword(s):  
Trichoderma Reesei ◽  
Scientific Literature ◽  
Large Body ◽  
Comprehensive Analysis ◽  
Transport Function ◽  
Sugar Transporters ◽  
New Knowledge ◽  
Electrophysiological Characterization ◽  
Shed Light

AbstractTrichoderma reesei is an ascomycete fungus known for its capability to secrete high amounts of extracellular cellulose- and hemicellulose-degrading enzymes. These enzymes are utilized in the production of second-generation biofuels and T. reesei is a well-established host for their production. Although this species has gained considerable interest in the scientific literature, the sugar transportome of T. reesei remains poorly characterized. Better understanding of the proteins involved in the transport of different sugars could be utilized for engineering better enzyme production strains. In this study we aimed to shed light on this matter by characterizing multiple T. reesei transporters capable of transporting various types of sugars. We used phylogenetics to select transporters for expression in Xenopus laevis oocytes to screen for transport activities. Of the 18 tested transporters, 8 were found to be functional in oocytes. 10 transporters in total were investigated in oocytes and in yeast, and for 3 of them no transport function had been described in literature. This comprehensive analysis provides a large body of new knowledge about T. reesei sugar transporters, and further establishes X. laevis oocytes as a valuable tool for studying fungal sugar transporters.

scholarly journals Homologous expression and characterization of Cel61A (EG IV) of Trichoderma reesei

2001 ◽  
Vol 268 (24) ◽  
pp. 6498-6507 ◽  
Author(s):  
Johan Karlsson ◽  
Markku Saloheimo ◽  
Matti Siika-aho ◽  
Maija Tenkanen ◽  
Merja Penttilä ◽  
...  
Keyword(s):  
Trichoderma Reesei ◽  
Homologous Expression

scholarly journals Production of Recombinant Trichoderma reesei Cellobiohydrolase II in a New Expression System Based on Wickerhamomyces anomalus

2017 ◽  
Vol 2017 ◽  
pp. 1-8 ◽  
Author(s):  
Dennis J. Díaz-Rincón ◽  
Ivonne Duque ◽  
Erika Osorio ◽  
Alexander Rodríguez-López ◽  
Angela Espejo-Mojica ◽  
...  
Keyword(s):  
Trichoderma Reesei ◽  
Recombinant Expression ◽  
Expression System ◽  
Enzymatic Extract ◽  
Native Strain ◽  
Wickerhamomyces Anomalus ◽  
Optimum Ph ◽  
Hydrolysis Of Cellulose ◽  
Cellobiohydrolase Ii ◽  
Hydrolysis Of

Cellulase is a family of at least three groups of enzymes that participate in the sequential hydrolysis of cellulose. Recombinant expression of cellulases might allow reducing their production times and increasing the low proteins concentrations obtained with filamentous fungi. In this study, we describe the production of Trichoderma reesei cellobiohydrolase II (CBHII) in a native strain of Wickerhamomyces anomalus. Recombinant CBHII was expressed in W. anomalus 54-A reaching enzyme activity values of up to 14.5 U L−1. The enzyme extract showed optimum pH and temperature of 5.0–6.0 and 40°C, respectively. Enzyme kinetic parameters (KM of 2.73 mM and Vmax of 23.1 µM min−1) were between the ranges of values reported for other CBHII enzymes. Finally, the results showed that an enzymatic extract of W. anomalus 54-A carrying the recombinant T. reesei CBHII allows production of reducing sugars similar to that of a crude extract from cellulolytic fungi. These results show the first report on the use of W. anomalus as a host to produce recombinant proteins. In addition, recombinant T. reesei CBHII enzyme could potentially be used in the degradation of lignocellulosic residues to produce bioethanol, based on its pH and temperature activity profile.

scholarly journals Enzymatic Properties and Intracellular Localization of the Novel Trichoderma reesei β-Glucosidase BGLII (Cel1A)

2002 ◽  
Vol 68 (9) ◽  
pp. 4546-4553 ◽  
Author(s):  
Markku Saloheimo ◽  
Juha Kuja-Panula ◽  
Erkko Ylösmäki ◽  
Michael Ward ◽  
Merja Penttilä
Keyword(s):  
Trichoderma Reesei ◽  
Culture Supernatant ◽  
Carbon Catabolite Repression ◽  
Intracellular Localization ◽  
Enzymatic Properties ◽  
The Novel ◽  
Transglycosylation Activity ◽  
Activity Measurements ◽  
Its Gene

ABSTRACT This paper describes the characterization of an intracellular β-glucosidase enzyme BGLII (Cel1a) and its gene (bgl2) from the cellulolytic fungus Trichoderma reesei (Hypocrea jecorina). The expression pattern of bgl2 is similar to that of other cellulase genes known from this fungus, and the gene would appear to be under the control of carbon catabolite repression mediated by the cre1 gene. The BGLII protein was produced in Escherichia coli, and its enzymatic properties were analyzed. It was shown to be a specific β-glucosidase, having no β-galactosidase side activity. It hydrolyzed both cellotriose and cellotetraose. BGLII exhibited transglycosylation activity, producing mainly cellotriose from cellobiose and sophorose and cellobiose from glucose. Antibodies raised against BGLII showed the presence of the enzyme in T. reesei cell lysates but not in the culture supernatant. Activity measurements and Western blot analysis of T. reesei strains expressing bgl2 from a constitutive promoter further confirmed the intracellular localization of this β-glucosidase.

Cellobiohydrolase II is the main conidial-bound cellulase in Trichoderma reesei and other Trichoderma strains

1991 ◽  
Vol 155 (6) ◽  
pp. 601-606 ◽  
Author(s):  
Robert Messner ◽  
Eva M. Kubicek-Pranz ◽  
Andrea Gsur ◽  
Christian P. Kubicek
Keyword(s):  
Trichoderma Reesei ◽  
Cellobiohydrolase Ii
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