Disulfide bonds elimination of endoglucanase II from Trichoderma reesei by site-directed mutagenesis to improve enzyme activity and thermal stability: An experimental and theoretical approach

2018 ◽  
Vol 120 ◽  
pp. 1572-1580 ◽  
Author(s):  
Ali Akbarzadeh ◽  
Navid Pourzardosht ◽  
Ehsan Dehnavi ◽  
Seyed Omid Ranaei Siadat ◽  
Mohammad Reza Zamani ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Enzyme Activity ◽  
Trichoderma Reesei ◽  
Theoretical Approach ◽  
Disulfide Bonds ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Endoglucanase Ii

scholarly journals Biochemical Characterization of Laboratory Mutants of Extended-Spectrum β-Lactamase TEM-60

2004 ◽  
Vol 48 (9) ◽  
pp. 3579-3582 ◽  
Author(s):  
Bibiana Caporale ◽  
Nicola Franceschini ◽  
Mariagrazia Perilli ◽  
Bernardetta Segatore ◽  
Gian Maria Rossolini ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Kinetic Parameters ◽  
Biochemical Characterization ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Extended Spectrum

ABSTRACT Three mutants of the extended-spectrum β-lactamase TEM-60, the P51L, K104E, and S164R mutants, were constructed by site-directed mutagenesis. The kinetic parameters of the mutated enzymes and interactions of inhibitors were significantly different from those of TEM-60, revealing that the L51P mutation plays an important role in enzyme activity and stability in the TEM-60 background.

Sign in / Sign up

Export Citation Format

Share Document