. Pong-bi-bi-mechanism-for-lower-substrate-concentrations, Interestingly, the kinetic data 359 corresponding to the O-acylation of (R)-2-butanol and (S)-2-butanol were found to fit with a steady-state ordered ternary complex bi-bi mechanism model. Concerning the 361 enantioselectivity studies, C. antarctica lipase B was found to preferentially catalyze (R)-2- 362 butanol O-acylation in terms of both catalytic activity and affinity: the calculated E-value of 363 3.17 confirmed its preferential enantioselectivity for (R)-enantiomer O-acylation, p.364

B. , E. L. Soo, A. B. Salleh, M. Basri, R. N. Rahman et al., sec-butylamine N-acylation seemed in fact to find its origin mostly in the 370 difference of catalysis rate and thus of catalytic activity rather than in the difference of affinity 371 toward the (R)-and (S)-enantiomers. Finally, it was confirmed that 372 C. antarctica lipase B is a chemoselective enzyme [2], exhibiting a preference for O-acylation 373 rather than for N-acylation, J. Biosci. 380 Bioeng. Tetrahedron, vol.953, issue.2, pp.361-367, 1997.

I. H. Segel-]-j, J. A. Straathof, F. Jongejan, S. Létisse, M. D. Lamare et al., 559-571. 402 [16] A. Fersht, Enzyme Structure and Mechanism, second ed., W. H. Freeman and 403 Company, Chem. Res. Enzyme Kinetics Enzyme Microb. Technol. Enzyme Microb. Technol. Biochim. Biophys. Acta BBA, vol.30, issue.15, pp.2355-2358, 1985.