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.

通过在无水条件下乙醇丁酸的酶催化酯化Ñ己烷，通过连续除去生成的水的，遵循一个乒乓双向双向反应机理; 将来自南极假丝酵母的固定化脂肪酶-B固定在丙烯酸​​树脂（Novozyme 435）上作为生物催化剂。首次，通过多参数非线性方程进行表面拟合处理了同时产生双死角底物抑制的酶促双底物反应的动力学数据。无水CH ₃ CH ₂ OH和/或CH ₃ CH ₂OD被用于尝试应用动力学同位素效应技术，并验证了可以描述上述反应的两个最佳系统（乒乓球Bi-bi和有序Bi-bi）的选择。