A kinetic model for the deactivation of pyruvate decarboxylase (PDC) by benzaldehyde
β Scribed by Y. S. Chow; H. S. Shin; A. A. Adesina; P. L. Rogers
- Publisher
- Springer Netherlands
- Year
- 1995
- Tongue
- English
- Weight
- 344 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0141-5492
No coin nor oath required. For personal study only.
β¦ Synopsis
To provide further understanding of the biotransformation of benzaldehyde to L-phenylaeetyl carbinol (L-PAC), an intermediate in L-ephedrine production, a kinetic model has been developed for the deactivation of pyruvate decarboxylase (PDC) by benzaldehyde. The model confirms that deactivation is first order with respect to benzaldehyde concentration and exhibits a square root dependency on time. The model covers the range of benzaldehyde concentrations 100-300 mM, as it has been shown previously that 200 mM benzaldehyde can produce L-PAC concentrations up to 190 mM (28.6 g/L) using partially purified PDC from Candida utilis.
π SIMILAR VOLUMES
Kinetic results on the glucoamylase-catalysed hydrolysis of maltose and maltotriose, and glucose polymerization into maltose and isomaltose up to 450 g/L total sugar concentration are presented. Whereas the enzyme has a faster hydrolytic and synthetic activity on ~(1'4) than on a-(I -6) linkages, at
A kinetic model of hydrocortisone transformation was developed in studies of the kinetics of biochemical systems. The regulatory bases of the model are the biosynthesis of steroid-transforming enzymes and their activity, the level of endogenous substrates, the respiratory chain activity, and the ini