Substrate Inhibition in Lipase-Catalysed Transesterification of Mandelic acid with Vinyl Acetate

Open access

Kinetic resolution of (R)- and (S)-mandelic acid by its transesterification with vinyl acetate catalysed by Burholderia cepacia lipase has been studied. The influence of the initial substrate concentration on the kinetics of process has been investigated. A modified ping-pong bi-bi model of enzymatic transesterification of (S)-mandelic acid including substrate inhibition has been developed. The values of kinetic parameters of the model have been estimated. We have shown that the inhibition effect revealed over a certain threshold limit value of the initial concentration of substrate.

Campbell R.F., Fitzpatric K., Inghardt T., Karlsson O., Nilsson K., Reilly J.E., Yet L., 2003. Enzymatic resolution of substituted mandelic acids. Tetrahedron Lett., 44, 5477-5481. DOI: 10.1016/S0040-4039(03)01270-X.

Dąbkowska K., Szewczyk K.W., 2007. Mathematical modelling of enzymatic transesterification of mandelic acid with vinyl acetate. Chem. Proc. Eng., 28, 795-802.

Dąbkowska K., Szewczyk K.W., 2009. Influence of temperature on the activity and enantioselectivity of Burkholderia cepacia lipase in the kinetic resolution of mandelic acid enantiomers. Biochem. Eng. J., 46, 147- 153. DOI: 10.1016/j.bej.2009.04.023.

Ghanem A., Aboul-Enein H.Y., 2005. Application of lipases in kinetic resolution of racemates. Chirality, 17, 1-15. DOI: 10.1002/chir.20089.

Gröger H., 2001. Enzymatic Routes to Enantiomerically pure aromatic α-hydroxy carboxylic acids: A further example for the diversity of biocatalysis. Adv. Synth. Catal., 343, 547-558. DOI: 10.1002/1615- 4169(200108)343:6/7<547::AID-ADSC547>3.0.CO;2-A.

Kibara K., Sakai K., Hashimoto Y., Nohira H., Saigo K., 1996. Design of resolving reagents: p-substituted mandelic acid as resolving reagents for 1-arylalkylamines. Tetrahedron: Asymmetry, 7, 1539-1542. DOI: 10.1016/0957-4166(96)00175-9.

Maier N.M., Franco P., Lindner W., 2001. Separation of enantiomers: needs, challenges, perspectives. J. Chromatogr. A, 906, 3-33. DOI: 10.1016/S0021-9673(00)00532-X.

Palomo M., Fernandez-Lorente G., Mateo C., Ortiz C., Guisan J.M., Fernandez-Lafuente R., 2002. Modulation of the enantioselectivity of lipases via controlled immobilization and medium engineering: hydrolytic resolution of mandelic acid esters. Enz. Microb. Technol., 31, 775-783. DOI: 10.1016/S0141-0229(02)00169-2.

Pilarek M., Szewczyk K.W., 2007. Kinetic model of 1,3-specific triacylglycerols alcoholysis catalyzed by lipases. J. Biotechnol., 127, 736-744. DOI: 10.1016/j.jbiotec.2006.08.012.

Segel I.H., 1993. Enzyme kinetic. Behavior and analysis of rapid equilibrium and steady-state enzyme systems. Wiley, New York, 827-828.

Sharma D., Sharma B., Shukla A.K., 2011. Biotechnological approach of microbial lipase: A review. Biotechnology, 10, 23-40. DOI: 10.3923/biotech.2011.23.40.

Stinson C.S., 2001. Chiral pharmaceuticals. Chem. Eng. News, 79, 79-97. DOI: 10.1021/cen-v079n040.p079.

Surivet J.-P., Vatèle J.-M., 1998. First total synthesis of (-)-8-epi-9-deoxygoniopypyrone. Tetrahedron Lett., 39, 9681-9682. DOI: 10.1016/S0040-4039(98)02269-2.

Szewczyk K.W., Pilarek M., Wrona M., 2001. Enzymatic propanolysis of triacetin. Inż. Chem. Proc., 22, 1351-1356.

Terreni M., Pagani G., Ubiali D., Fernández-Lafuente R., Mateo C., Guisán J.M., 2001. Modulation of penicillin acylase properties via immobilization techniques: one-pot chemoenzymatic synthesis of caphamandole from cephalosporin C. Bioorg. Med. Chem. Lett., 11, 2429-2432. DOI: 10.1016/S0960-894X(01)00463-2. Queiroz N., Nascimento M. G., 2002. Pseudomonas sp. lipase immobilized in polymers versus the use of free enzyme in the resolution of (R,S)-methyl mandelate. Tetrahedron Lett., 43, 5225-5227. DOI: 10.1016/S0040- 4039(02)01057-2.

Yadav G.D., Sivakumar P., 2004. Enzyme-catalysed optical resolution of mandelic acid via (R,S)-methyl mandelate in non-aqueous media. Biochem. Eng. J., 19, 101-107. DOI: 10.1016/j.bej.2003.12.004.

Chemical and Process Engineering

The Journal of Committee of Chemical and Process of Polish Academy of Sciences

Journal Information

IMPACT FACTOR 2016: 0.971

CiteScore 2016: 1.03

SCImago Journal Rank (SJR) 2016: 0.395
Source Normalized Impact per Paper (SNIP) 2016: 0.873


All Time Past Year Past 30 Days
Abstract Views 0 0 0
Full Text Views 43 43 15
PDF Downloads 10 10 3