Substrate specificity of enzymes in organic solvents vs. water is reversed

1986 ◽  
Vol 108 (10) ◽  
pp. 2767-2768 ◽  
Author(s):  
Aleksey. Zaks ◽  
Alexander M. Klibanov
1996 ◽  
Vol 118 (51) ◽  
pp. 12891-12901 ◽  
Author(s):  
Apurva K. Chaudhary ◽  
Sanjay V. Kamat ◽  
Eric J. Beckman ◽  
David Nurok ◽  
Robert M. Kleyle ◽  
...  

2010 ◽  
Vol 76 (12) ◽  
pp. 4096-4098 ◽  
Author(s):  
Tatiana N. Stekhanova ◽  
Andrey V. Mardanov ◽  
Ekaterina Y. Bezsudnova ◽  
Vadim M. Gumerov ◽  
Nikolai V. Ravin ◽  
...  

ABSTRACT Short-chain alcohol dehydrogenase, encoded by the gene Tsib_0319 from the hyperthermophilic archaeon Thermococcus sibiricus, was expressed in Escherichia coli, purified and characterized as an NADPH-dependent enantioselective oxidoreductase with broad substrate specificity. The enzyme exhibits extremely high thermophilicity, thermostability, and tolerance to organic solvents and salts.


2018 ◽  
Vol 18 (6) ◽  
pp. 61-73 ◽  
Author(s):  
Yu. V. Samoilova ◽  
K. N. Sorokina ◽  
A. V. Piligaev ◽  
V. N. Parmon

In the review paper, the modern investigations on the application of thermostable lipolytic bacterial enzymes for biotechnology are discussed, the properties of these enzymes discussed including their activity and functional stability at various temperatures, pH in organic solvents, as well as the substrate specificity and activity in the presence of various chemical compounds. The paper contains data on the development of recombinant producers of lipolytic bacterial enzymes and on approaches to improving their productivity. The application of the bacterial lipases for biotechnological processes of synthesis of biofuel, various chemicals and detergents, for food industry and wastewater treatment is considered.


Sign in / Sign up

Export Citation Format

Share Document