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7743502 
Journal Article 
New insights and tools for the elucidation of lipase catalyzed esterification reaction mechanism in n-hexane: The synthesis of ethyl butyrate 
Foukis, A; Gkini, OA; Stergiou, PY; Papamichael, EM 
2018 
1 
Molecular Catalysis
ISSN: 2468-8231 
Elsevier B.V. 
455 
159-163 
English 
WOS:000442191400019 
The enzyme catalyzed esterification of butyric acid by ethanol under anhydrous conditions in n-hexane, through continuous removal of the formed water, follows a ping pong bi-bi reaction mechanism; immobilized lipase-B from Candida antarctica on acrylic resin (Novozyme 435) was used as biocatalyst. For first time, the kinetic data of an enzymatic bi-substrate reaction generating simultaneous double dead-end substrate inhibitions were processed by surface fitting through multiparametric non-linear equations. Both anhydrous CH3CH2OH and/or CH3CH2OD were employed in an attempt to apply the technique of kinetic isotope effects and validate the selection of the best system among two (ping pong bi-bi and ordered bi-bi), which could describe the aforementioned reaction. © 2018 Elsevier B.V. 
Ethyl butyrate; Lipase-catalyzed esterification kinetics; Surface fitting; Kinetic isotope effect; Ping pang bi-bi mechanism