A Model Explaining Declining Rate in Hydrolysis of Lignocellulose Substrates with Cellobiohydrolase I (Cel7A) and Endoglucanase I (Cel7B) of Trichoderma reesei

2002 ◽  
Vol 101 (1) ◽  
pp. 41-60 ◽  
Author(s):  
Torny Eriksson ◽  
Johan Karlsson ◽  
Folke Tjerneld
Keyword(s):  
Trichoderma Reesei ◽  
Cellobiohydrolase I ◽  
Endoglucanase I ◽  
Hydrolysis Of

scholarly journals Enhancing Enzymatic Properties of Endoglucanase I Enzyme from Trichoderma Reesei via Swapping from Cellobiohydrolase I Enzyme

Catalysts ◽  
2019 ◽  
Vol 9 (2) ◽  
pp. 130 ◽  
Author(s):  
Aslı Yenenler ◽  
Hasan Kurt ◽  
Osman Sezerman
Keyword(s):  
Thermal Stability ◽  
Enzymatic Activity ◽  
Trichoderma Reesei ◽  
Metal Ion ◽  
Structural Integrity ◽  
Green Energy ◽  
Cellobiohydrolase I ◽  
Endoglucanase I ◽  
The Difference ◽  
Spectroscopy Studies

Utilizing plant-based materials as a biofuel source is an increasingly popular attempt to redesign the global energy cycle. This endeavour underlines the potential of cellulase enzymes for green energy production and requires the structural and functional engineering of natural enzymes to enhance their utilization. In this work, we aimed to engineer enzymatic and functional properties of Endoglucanase I (EGI) by swapping the Ala43-Gly83 region of Cellobiohydrolase I (CBHI) from Trichoderma reesei. Herein, we report the enhanced enzymatic activity and improved thermal stability of the engineered enzyme, called EGI_swapped, compared to EGI. The difference in the enzymatic activity profile of EGI_swapped and the EGI enzymes became more pronounced upon increasing metal-ion concentrations in the reaction media. Notably, the engineered enzyme retained a considerable level of enzymatic activity after thermal incubation for 90 min at 70 °C while EGI completely lost its enzymatic activity. Circular Dichroism spectroscopy studies revealed distinctive conformational and thermal susceptibility differences between EGI_swapped and EGI enzymes, confirming the improved structural integrity of the swapped enzyme. This study highlights the importance of swapping the metal-ion coordination region in the engineering of EGI enzyme for enhanced structural and thermal stability.

scholarly journals Hydrolyses of α- and β-cellobiosyl fluorides by cellobiohydrolases of Trichoderma reesei

1993 ◽  
Vol 291 (3) ◽  
pp. 883-888 ◽  
Author(s):  
A K Konstantinidis ◽  
I Marsden ◽  
M L Sinnott
Keyword(s):  
Trichoderma Reesei ◽  
Biological Function ◽  
Fluoride Ion ◽  
Cellobiohydrolase I ◽  
Ion Release ◽  
Cellulase Complex ◽  
Cellobiohydrolase Ii ◽  
Glycoside Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of

Cellobiohydrolase II hydrolyses alpha- and beta-D-cellobiosyl fluorides to alpha-cellobiose at comparable rates, according to Michaelis-Menten kinetics. The stereochemistry, absence of transfer products and strict hyperbolic kinetics of the hydrolysis of alpha-cellobiosyl fluoride suggest that the mechanism for the alpha-fluoride may be the enzymic counterpart of the SNi reaction observed in the trifluoroethanolysis of alpha-glucopyranosyl fluoride [Sinnott and Jencks (1980) J. Am. Chem. Soc. 102, 2026-2032]. The absolute factors by which this enzyme accelerates fluoride ion release are small and greater for the alpha-fluoride than for the beta, suggesting that its biological function may not be just glycoside hydrolysis. Cellobiohydrolase I hydrolyses only beta-cellobiosyl fluoride, which is, however, an approx. 1-3% contaminant in alpha-cellobiosyl fluoride as prepared and purified by conventional methods. Instrumental assays for the various components of the cellulase complex are discussed.

scholarly journals Mechanisms of thermoinactivation of endoglucanase I from Trichoderma reesei QM 9414

1992 ◽  
Vol 287 (2) ◽  
pp. 583-588 ◽  
Author(s):  
J M Dominguez ◽  
C Acebal ◽  
J Jimenez ◽  
I de la Mata ◽  
R Macarron ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Trichoderma Reesei ◽  
Time Course ◽  
Enzyme Concentration ◽  
Main Process ◽  
Peptide Bonds ◽  
First Order ◽  
First Order Kinetics ◽  
Endoglucanase I ◽  
Hydrolysis Of

The mechanism of irreversible thermoinactivation of endoglucanase I from Trichoderma reesei has been determined at 70 degrees C at the pH of maximum enzyme activity. The time-course of thermoinactivation did not follow first-order kinetics and kinetic constants of the process were dependent on enzyme concentration, suggesting that aggregation was the main process leading to irreversible inactivation. The enzyme was extremely resistant to urea, which in fact seemed to stabilize it against temperature. Disulphide exchange, deamidation and hydrolysis of peptide bonds were also responsible for the loss of enzyme activity at 70 degrees C.

scholarly journals Visualization of Trichoderma reesei Cellobiohydrolase I and Endoglucanase I on Aspen Cellulose by Using Monoclonal Antibody-Colloidal Gold Conjugates

1991 ◽  
Vol 57 (11) ◽  
pp. 3163-3170 ◽  
Author(s):  
Rafael A. Nieves ◽  
Robert P. Ellis ◽  
Roberta J. Todd ◽  
Timothy J. A. Johnson ◽  
Karel Grohmann ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Trichoderma Reesei ◽  
Colloidal Gold ◽  
Cellobiohydrolase I ◽  
Endoglucanase 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
Sign in / Sign up

Export Citation Format

Share Document