| Title : A kinetic study of immobilized lipase catalysing the synthesis of isoamyl acetate by transesterification in n-hexane - Rizzi_1992_Enzyme.Microb.Technol_14_709 |
| Author(s) : Rizzi M , Stylos P , Riek A , Reuss M |
| Ref : Enzyme Microb Technol , 14 :709 , 1992 |
|
Abstract :
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. |
| PubMedSearch : Rizzi_1992_Enzyme.Microb.Technol_14_709 |
| PubMedID: 1368893 |
| Substrate | 3-methyl-butylacetate |
Rizzi M, Stylos P, Riek A, Reuss M (1992)
A kinetic study of immobilized lipase catalysing the synthesis of isoamyl acetate by transesterification in n-hexane
Enzyme Microb Technol
14 :709
Rizzi M, Stylos P, Riek A, Reuss M (1992)
Enzyme Microb Technol
14 :709