Enantiomeric resolution of 2-aryl propionic esters with hyperthermophilic and mesophilic esterases: contrasting thermodynamic mechanisms.
The enantiomeric resolution of 2-aryl propionic esters by hyperthermophilic and mesophilic esterases was found to be governed by contrasting thermodynamic mechanisms. Entropic contributions predominated for mesophilic esterases from Candida rugosa and Rhizomucor miehei, while enthalpic forces controlled this resolution by the esterase from the extremely thermoacidophilic archaeon, Sulfolobus solfataricus P1. This disparity in thermodynamic mechanism can be attributed to the differences in conformational flexibility of mesophilic and thermophilic enzymes as they relate to the temperature range (4-70 degrees C) examined.
Sehgal
Amitabh C
AC
Department of Chemical Engineering, North Carolina State University, Raleigh, North Carolina 27695-7905, USA.
Kelly
Robert M
RM
D002175:Candida / Q000201:enzymology; D043182:Carboxylesterase; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry; D004950:Esterases / Q000737:chemistry*; D004952:Esters / Q000737:chemistry / Q000302:isolation & purification; D008049:Lipase / Q000737:chemistry; D009288:Naproxen / Q000737:chemistry / Q000302:isolation & purification; D011422:Propionates / Q000737:chemistry / Q000302:isolation & purification*; D020103:Rhizomucor / Q000201:enzymology*; D013237:Stereoisomerism; D013379:Substrate Specificity; D016944:Sulfolobus / Q000201:enzymology; D013816:Thermodynamics
D004952:Esters; D011422:Propionates; D009288:Naproxen; D004950:Esterases; D002265:Carboxylic Ester Hydrolases; D043182:Carboxylesterase; D008049:Lipase