A kinetic study of immobilized lipase catalysing the synthesis of isoamyl acetate by transesterification in n-hexane.
Isoamyl acetate was synthesized by lipase-catalyzed transesterification of ethyl acetate in n-hexane. The selectivity and rates of ester formation decreased when water content of the immobilized enzyme exceeded 3% (w/w). Experimental observations clearly indicate that the substrates as well as the product (ethanol) act as dead-end inhibitors. A ping-pong bi-bi mechanism with competitive inhibition by substrates and products is proposed that predicts the experimental observation satisfactorily.
Rizzi
M
M
Institut für Bioverfahrenstechnik, Universität Stuttgart, Germany.
Stylos
P
P
Riek
A
A
Reuss
M
M
D004800:Enzymes, Immobilized / Q000378:metabolism*; D004951:Esterification; D006586:Hexanes; D008049:Lipase / Q000378:metabolism*; D008956:Models, Chemical; D000439:Pentanols
D004800:Enzymes, Immobilized; D006586:Hexanes; D000439:Pentanols; C026385:n-hexane; D008049:Lipase; C020377:isoamyl acetate