2000
DOI: 10.1002/1097-4660(200008)75:8<707::aid-jctb278>3.0.co;2-3
|View full text |Cite
|
Sign up to set email alerts
|

Kinetic study of the enantioselective hydrolysis of a meso-diester using pig liver esterase

Abstract: A kinetic study of the hydrolysis of the diester dimethyl cis-cyclohex-4-ene-1,2-dicarboxylate, to the (1S,2R)-monoester, catalysed by the enzyme Pig Liver Esterase (PLE) was performed. The effects of the most relevant parameters that in¯uence the enzymatic conversion were studied, such as pH, temperature and concentration of substrate and reaction products. It was concluded that the pH at which the enzyme exhibits a maximum activity is pH 7. At 25°C PLE presents a better long-term stability and enantioselecti… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

0
6
0

Year Published

2002
2002
2018
2018

Publication Types

Select...
5
2

Relationship

0
7

Authors

Journals

citations
Cited by 10 publications
(6 citation statements)
references
References 24 publications
(22 reference statements)
0
6
0
Order By: Relevance
“…The other enantiomer, (1 S ,2 R) -monoester 2a , was repeatedly synthesized via a pig liver esterase-catalyzed reaction. Unfortunately the reaction is not entirely enantioselective, and a lower enantiomeric excess of 80–97% ee was obtained (Scheme ). , The reduced enantioselectivity results from the presence of several parallel hydrolytic reactions, each independently catalyzed by different isoenzymes of pig liver esterase. The products of highly enantioselective isoenzymes are hereby mixed with products from less selective enzymes.…”
Section: Results and Discussionmentioning
confidence: 99%
“…The other enantiomer, (1 S ,2 R) -monoester 2a , was repeatedly synthesized via a pig liver esterase-catalyzed reaction. Unfortunately the reaction is not entirely enantioselective, and a lower enantiomeric excess of 80–97% ee was obtained (Scheme ). , The reduced enantioselectivity results from the presence of several parallel hydrolytic reactions, each independently catalyzed by different isoenzymes of pig liver esterase. The products of highly enantioselective isoenzymes are hereby mixed with products from less selective enzymes.…”
Section: Results and Discussionmentioning
confidence: 99%
“…The radiolytic decomposition of a given antibiotic can be described using the Monod equation (equation 3), frequently used in enzyme kinetic studies [25,26,27,28,29,30].…”
Section: Determination Of Kinetic Parameters Of the Monod Equationmentioning
confidence: 99%
“…The differential material balance for the diester in the aqueous film of thickness δ aq can be written as where C A(aq) is the diester concentration in the aqueous film, D A(aq) is the diffusion coefficient of the diester in the aqueous phase, and r A(aq) ≡ r A ( C A(aq) , C B(aq) ) is the reaction rate in the aqueous film, expressed as consumption of A. As shown by Sousa et al, r A is well described by a Michaelis−Menten kinetics with noncompetitive inhibition by methanol: The values of the kinetic parameters are V max = 1.28 × 10 - 8 (M enz unit -1 s -1 ) × enz unit, K M = 0.044 M, and K I = 1.93 M. Taking into consideration the stoichiometry of the enzymatic reaction, the concentration of methanol, C I , is equal to the concentration of monoester, C B .…”
Section: Model Developmentmentioning
confidence: 99%
“…The differential material balance for the diester in the aqueous film of thickness δ aq can be written as where C A(aq) is the diester concentration in the aqueous film, D A(aq) is the diffusion coefficient of the diester in the aqueous phase, and r A(aq) ≡ r A (C A(aq) ,C B(aq) ) is the reaction rate in the aqueous film, expressed as consumption of A. As shown by Sousa et al, 11 r A is well described by a Michaelis-Menten kinetics with noncompetitive inhibition by methanol:…”
Section: Model Developmentmentioning
confidence: 99%