Details
| Original language | English |
|---|---|
| Pages (from-to) | 1532-1547 |
| Number of pages | 16 |
| Journal | Journal of mathematical chemistry |
| Volume | 51 |
| Issue number | 6 |
| Publication status | Published - 28 Mar 2013 |
Abstract
A mathematical model is presented for the kinetic resolution of racemates. It takes all intermediate binding steps into account and assumes that such steps are reversible. The model describing dynamics of the chiral reaction products consists of two nonlinear differential equations. With this model, the enantioselectivity of enzyme has been studied. Mathematical and numerical simulation of the model show that there are several ways to control the enantiomeric ratio (E) but the affinity and the binding rates of the intermediate enzyme complex to the racemic substrates are the key steps for the enzyme enantioselectivity.
Keywords
- Enantioselectivity, Kinetic resolution of racemate, Lipase, Mathematical modeling, Organic solvent, Transesterification
ASJC Scopus subject areas
- Chemistry(all)
- General Chemistry
- Mathematics(all)
- Applied Mathematics
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In: Journal of mathematical chemistry, Vol. 51, No. 6, 28.03.2013, p. 1532-1547.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - A new mathematical model for the enzymatic kinetic resolution of racemates
AU - Aydemir, Adnan
AU - Yildirim, Necmettin
AU - Hitzmann, Bernd
AU - Scheper, Thomas
PY - 2013/3/28
Y1 - 2013/3/28
N2 - A mathematical model is presented for the kinetic resolution of racemates. It takes all intermediate binding steps into account and assumes that such steps are reversible. The model describing dynamics of the chiral reaction products consists of two nonlinear differential equations. With this model, the enantioselectivity of enzyme has been studied. Mathematical and numerical simulation of the model show that there are several ways to control the enantiomeric ratio (E) but the affinity and the binding rates of the intermediate enzyme complex to the racemic substrates are the key steps for the enzyme enantioselectivity.
AB - A mathematical model is presented for the kinetic resolution of racemates. It takes all intermediate binding steps into account and assumes that such steps are reversible. The model describing dynamics of the chiral reaction products consists of two nonlinear differential equations. With this model, the enantioselectivity of enzyme has been studied. Mathematical and numerical simulation of the model show that there are several ways to control the enantiomeric ratio (E) but the affinity and the binding rates of the intermediate enzyme complex to the racemic substrates are the key steps for the enzyme enantioselectivity.
KW - Enantioselectivity
KW - Kinetic resolution of racemate
KW - Lipase
KW - Mathematical modeling
KW - Organic solvent
KW - Transesterification
UR - http://www.scopus.com/inward/record.url?scp=84876964428&partnerID=8YFLogxK
U2 - 10.1007/s10910-013-0162-7
DO - 10.1007/s10910-013-0162-7
M3 - Article
AN - SCOPUS:84876964428
VL - 51
SP - 1532
EP - 1547
JO - Journal of mathematical chemistry
JF - Journal of mathematical chemistry
SN - 0259-9791
IS - 6
ER -