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Advantages of using non-isothermal bioreactors for the enzymatic synthesis of antibiotics: the penicillin G acylase as enzyme model.
- Source :
-
Biotechnology and bioengineering [Biotechnol Bioeng] 2002 Aug 05; Vol. 79 (3), pp. 334-46. - Publication Year :
- 2002
-
Abstract
- A new hydrophobic and catalytic membrane was prepared by immobilizing Penicillin G acylase (PGA, EC.3.5.1.11) from E. coli on a nylon membrane, chemically grafted with butylmethacrylate (BMA). Hexamethylenediamine (HMDA) and glutaraldehyde (Glu) were used as a spacer and coupling agent, respectively. PGA was used for the enzymatic synthesis of cephalexin, using D(-)-phenylglycine methyl ester (PGME) and 7-amino-3-deacetoxycephalosporanic acid (7-ADCA) as substrates. Several factors affecting this reaction, such as pH, temperature, and concentrations of substrates were investigated. The results indicated good enzyme-binding efficiency of the pre-treated membrane, and an increased stability of the immobilized PGA towards pH and temperature. Calculation of the activation energies showed that cephalexin production by the immobilized biocatalyst was limited by diffusion, resulting in a decrease of enzyme activity and substrate affinity. Temperature gradients were employed as a way to reduce the effects of diffusion limitation. Cephalexin was found to linearly increase with the applied temperature gradient. A temperature difference of about 3 degrees C across the catalytic membrane resulted into a cephalexin synthesis increase of 100% with a 50% reduction of the production times. The advantage of using non-isothermal bioreactors in biotechnological processes, including pharmaceutical applications, is also discussed.<br /> (Copyright 2002 Wiley Periodicals, Inc.)
- Subjects :
- Catalysis
Cephalosporins chemistry
Coated Materials, Biocompatible
Enzymes, Immobilized
Equipment Design
Escherichia coli enzymology
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Methacrylates
Models, Chemical
Propylene Glycols chemistry
Sensitivity and Specificity
Temperature
Anti-Bacterial Agents chemical synthesis
Bioreactors
Cephalexin chemical synthesis
Membranes, Artificial
Nylons
Penicillin Amidase chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3592
- Volume :
- 79
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biotechnology and bioengineering
- Publication Type :
- Academic Journal
- Accession number :
- 12115422
- Full Text :
- https://doi.org/10.1002/bit.10303