TY - JOUR
T1 - Characterization and optimization of carboxylesterase-catalyzed esterification between capric acid and glycerol for the production of 1-monocaprin in reversed micellar system
AU - Park, Kyung Min
AU - Kwon, Oh Taek
AU - Ahn, Seon Min
AU - Lee, Jae Hwan
AU - Chang, Pahn Shick
PY - 2010/12/31
Y1 - 2010/12/31
N2 - Calotropis procera R. Br. carboxylesterase (EC 3.1.1.1) solubilized in reversed micellar glycerol droplets containing a very small amount of water (less than 5ppm) and stabilized by a surfactant effectively catalyzed the esterification between glycerol and capric acid to produce 1-monocaprin. Reaction variables including surfactant types, organic solvent media, reaction time, G-value ([glycerol]/[capric acid]), R-value ([water]/[surfactant]), pH, temperature, and types of metal ion inhibitors on the carboxylesterase-catalyzed esterification were characterized and optimized to efficiently produce 1-monocaprin. Bis(2-ethylhexyl) sodium sulfosuccinate (AOT) and isooctane were the most effective surfactant and organic solvent medium, respectively, for 1-monocaprin formation in reversed micelles. The optimum G- and R-values were 3.0 and 0.05, respectively, and the optimum pH and temperature were determined to be 10.0 and 60°C, respectively. K m,app. and V max,app. were calculated from a Hanes-Woolf plot, and the values were 9.64mM and 2.45μM/minmg protein, respectively. Among various metal ions, Cu 2+ and Fe 2+ severely inhibited carboxylesterase-catalyzed esterification activity (less than 6.0% of relative activity).
AB - Calotropis procera R. Br. carboxylesterase (EC 3.1.1.1) solubilized in reversed micellar glycerol droplets containing a very small amount of water (less than 5ppm) and stabilized by a surfactant effectively catalyzed the esterification between glycerol and capric acid to produce 1-monocaprin. Reaction variables including surfactant types, organic solvent media, reaction time, G-value ([glycerol]/[capric acid]), R-value ([water]/[surfactant]), pH, temperature, and types of metal ion inhibitors on the carboxylesterase-catalyzed esterification were characterized and optimized to efficiently produce 1-monocaprin. Bis(2-ethylhexyl) sodium sulfosuccinate (AOT) and isooctane were the most effective surfactant and organic solvent medium, respectively, for 1-monocaprin formation in reversed micelles. The optimum G- and R-values were 3.0 and 0.05, respectively, and the optimum pH and temperature were determined to be 10.0 and 60°C, respectively. K m,app. and V max,app. were calculated from a Hanes-Woolf plot, and the values were 9.64mM and 2.45μM/minmg protein, respectively. Among various metal ions, Cu 2+ and Fe 2+ severely inhibited carboxylesterase-catalyzed esterification activity (less than 6.0% of relative activity).
UR - https://www.scopus.com/pages/publications/77952471429
U2 - 10.1016/j.nbt.2009.11.004
DO - 10.1016/j.nbt.2009.11.004
M3 - Article
C2 - 19931658
AN - SCOPUS:77952471429
SN - 1871-6784
VL - 27
SP - 46
EP - 52
JO - New Biotechnology
JF - New Biotechnology
IS - 1
ER -