Direct transesterification of gases by "dry" immobilized lipase.
Several different reactor configurations, including single pass, continuous recycle, and batch reactor modes, were used to investigate the effects of temperature and water activity, or relative humidity, on lipase-catalyzed, gas-phase transesterifications. Temperature and relative humidity were controlled both inside reactors and throughout the course of the reaction to account for and optimize their effects. Results indicated that, at low relative humidity, reaction rates increased with temperature up to 60 degrees C. However, when relative humidity was increased, a similar increase in temperature resulted in the loss of nearly all enzyme activity. These results are consistent with the idea that enzymes without free water are more thermally stable. Furthermore, at constant ambient temperatures, production increased dramatically with an increase in relative humidity, confirming the idea that an increase in water activity increases catalytic activity. A mass balance performed on reactors at higher relative humidity revealed that hydrolysis (rather than transesterification) of the ester substrate could significantly decrease product yields.
Cameron
Paula A
PA
Chemical Technology Division, Oak Ridge National Laboratory, P.O. Box 2008, Oak Ridge, TN 37831-6226, USA.
Davison
Brian H
BH
Frymier
Paul D
PD
Barton
John W
JW
D000818:Animals; D019149:Bioreactors; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004951:Esterification; D005740:Gases / Q000737:chemistry / Q000378:metabolism*; D006813:Humidity; D008049:Lipase / Q000378:metabolism*; D000439:Pentanols / Q000378:metabolism*; D013379:Substrate Specificity; D013552:Swine; D013696:Temperature; D014867:Water
D004800:Enzymes, Immobilized; D005740:Gases; D000439:Pentanols; D014867:Water; D008049:Lipase; C020377:isoamyl acetate