Adsorption and Activity of Trichoderma reesei Cellobiohydrolase I, Endoglucanase II, and the Corresponding Core Proteins on Steam Pretreated Willow

1999 ◽  
Vol 81 (2) ◽  
pp. 81-90 ◽  
Author(s):  
Pia Kotiranta ◽  
Johan Karlsson ◽  
Matti Siika-Aho ◽  
József Medve ◽  
Liisa Viikari ◽  
...  
Keyword(s):  
Trichoderma Reesei ◽  
Cellobiohydrolase I ◽  
Endoglucanase Ii ◽  
Core Proteins

scholarly journals Enhanced Production of Trichoderma reesei Endoglucanases and Use of the New Cellulase Preparations in Producing the Stonewashed Effect on Denim Fabric

2002 ◽  
Vol 68 (8) ◽  
pp. 3956-3964 ◽  
Author(s):  
Arja Miettinen-Oinonen ◽  
Pirkko Suominen
Keyword(s):  
Trichoderma Reesei ◽  
Copy Number ◽  
Parent Strain ◽  
Expression Cassette ◽  
Coding Region ◽  
Cellobiohydrolase I ◽  
Endoglucanase Activity ◽  
Endoglucanase Ii ◽  
Enhanced Production ◽  
Denim Fabric

ABSTRACT Trichoderma reesei strains were constructed for production of elevated amounts of endoglucanase II (EGII) with or without cellobiohydrolase I (CBHI). The endoglucanase activity produced by the EGII transformants correlated with the copy number of the egl2 expression cassette. One copy of the egl2 expression cassette in which the egl2 was under the cbh1 promoter increased production of endoglucanase activity 2.3-fold, and two copies increased production about 3-fold above that of the parent strain. When the enzyme with elevated EGII content was used, an improved stonewashing effect on denim fabric was achieved. A T. reesei strain producing high amounts of EGI and -II activities without CBHI and -II was constructed by replacing the cbh2 locus with the coding region of the egl2 gene in the EGI-overproducing CBHI-negative strain. Production of endoglucanase activity by the EG-transformant strain was increased fourfold above that of the host strain. The filter paper-degrading activity of the endoglucanase-overproducing strain was lowered to below detection, presumably because of the lack of cellobiohydrolases.

scholarly journals Cellulose hydrolysis by the cellulases from Trichoderma reesei: adsorptions of two cellobiohydrolases, two endocellulases and their core proteins on filter paper and their relation to hydrolysis

1994 ◽  
Vol 303 (3) ◽  
pp. 817-823 ◽  
Author(s):  
B Nidetzky ◽  
W Steiner ◽  
M Claeyssens
Keyword(s):  
Mass Transfer ◽  
Trichoderma Reesei ◽  
Filter Paper ◽  
Cellulose Hydrolysis ◽  
Solid Substrate ◽  
Bulk Liquid ◽  
Cellobiohydrolase I ◽  
Irreversible Adsorption ◽  
Core Proteins ◽  
Cellulose Binding

Separate binding of several purified cellulolytic components of Trichoderma reesei on to filter paper was studied and concomitant hydrolysis rates evaluated. Enhancement of mass transfer from the bulk liquid to the solid substrate by agitation has two different effects on adsorption depending on the type of enzyme: (i) the fraction of cellobiohydrolase II (CBH II) and endoglucanase III (EG III) bound at equilibrium is increased, whereas (ii) the rate but not the extent of cellobiohydrolase I (CBH I) and endoglucanase I (EG I) adsorption is affected. The adsorption of CBH I core, a component lacking the cellulose-binding domain (CBD), is, however, not significantly influenced by mass transfer. The CBH I interdomain peptide (present in CBH I core b) does not participate in adsorption but enhances stability. The adsorption of CBH I core proteins is a fully reversible process whereas that of the intact CBH I is not. Thus, the interaction of the CBD with filter paper apparently accounts for the mass-transfer-limited binding rate and also for the irreversible adsorption of intact CBH I. Adsorption isotherms at 50 degrees C indicate very similar relative association constants for the intact cellulases (0.24-0.30 l/g of cellulose), but drastically reduced values for CBH I core proteins (0.03 l/g of cellulose). The specific activities of adsorbed CBH I and of its core proteins are identical and a linear relationship between adsorption and rates of hydrolysis is found only for these enzymes. Thus, non-productive binding on to cellulose seems evident in the case of CBH II and EG III but not CBH I.

Crystallization and Preliminary X-ray Studies on the Core Proteins of Cellobiohydrolase I and Endoglucanase I from Trichoderma reesei

1993 ◽  
Vol 234 (3) ◽  
pp. 905-907 ◽  
Author(s):  
Christina Divne ◽  
Irmgard Sinning ◽  
Jerry Ståhlberg ◽  
Göran Pettersson ◽  
Michael Bailey ◽  
...  
Keyword(s):  
Trichoderma Reesei ◽  
Cellobiohydrolase I ◽  
X Ray ◽  
The Core ◽  
Core Proteins ◽  
Endoglucanase I

The diversity of glycosylation of cellobiohydrolase I from Trichoderma reesei determined with mass spectrometry

2019 ◽  
Vol 508 (3) ◽  
pp. 818-824 ◽  
Author(s):  
Mingyu Wang ◽  
Yanan Ma ◽  
Ling Li ◽  
Bianfang Wang ◽  
Xin Wei ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Trichoderma Reesei ◽  
Cellobiohydrolase I

scholarly journals Expression and secretion of fungal endoglucanase II and chimeric cellobiohydrolase I in the oleaginous yeast Lipomyces starkeyi

2017 ◽  
Vol 16 (1) ◽  
Author(s):  
Qi Xu ◽  
Eric P. Knoshaug ◽  
Wei Wang ◽  
Markus Alahuhta ◽  
John O. Baker ◽  
...  
Keyword(s):  
Oleaginous Yeast ◽  
Lipomyces Starkeyi ◽  
Cellobiohydrolase I ◽  
Endoglucanase Ii

Cellobiose metabolism and cellobiohydrolase I biosynthesis by Trichoderma reesei

1990 ◽  
Vol 14 (4) ◽  
pp. 405-415 ◽  
Author(s):  
C. Fritscher ◽  
R. Messner ◽  
C.P. Kubicek
Keyword(s):  
Trichoderma Reesei ◽  
Cellobiohydrolase I ◽  
Cellobiose Metabolism
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