Enzymatic processes for fine chemicals and pharmaceuticals: Kinetic simulation for optimal R-phenylacetylcarbinol production
An optimal feeding strategy with a 1:1.2 molar ratio of benzaldehyde: pyruvate has been developed to maximize the enzymatic production of the pharmaceutical intermediate R-phenylacetylcarbinol (PAC) based on a previously published model for this intermediate. The results of the simulation indicate w...
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th-cmuir.6653943832-5702014-08-29T08:50:23Z Enzymatic processes for fine chemicals and pharmaceuticals: Kinetic simulation for optimal R-phenylacetylcarbinol production Leksawasdi N. Rosche B. Rogers P. An optimal feeding strategy with a 1:1.2 molar ratio of benzaldehyde: pyruvate has been developed to maximize the enzymatic production of the pharmaceutical intermediate R-phenylacetylcarbinol (PAC) based on a previously published model for this intermediate. The results of the simulation indicate with pyruvate decarboxylase (PDC) at an initial carboligase activity of 4 U ml-1 that up to 730 mM PAC would be produced in 81 h. However, the experimental results show an appreciably lower maximum level of PAC (viz 300 mM) produced after only 54 h, although enzyme activity was maintained at similar or higher values than in the simulation results. It is possible that the increasing PAC concentrations and associated by-products (acetoin and acetaldehyde) have resulted in significant inhibition of PDC during the course of the biotransformation and future model development will need to include one or more product inhibition terms in its structure. © 2006 Elsevier B.V. All rights reserved. 2014-08-29T08:50:23Z 2014-08-29T08:50:23Z 2006 Conference Paper 01672991 SSCTD http://www.scopus.com/inward/record.url?eid=2-s2.0-33745783275&partnerID=40&md5=2aaf5b88099a98110e1dcd80b22ae198 http://cmuir.cmu.ac.th/handle/6653943832/570 English |
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An optimal feeding strategy with a 1:1.2 molar ratio of benzaldehyde: pyruvate has been developed to maximize the enzymatic production of the pharmaceutical intermediate R-phenylacetylcarbinol (PAC) based on a previously published model for this intermediate. The results of the simulation indicate with pyruvate decarboxylase (PDC) at an initial carboligase activity of 4 U ml-1 that up to 730 mM PAC would be produced in 81 h. However, the experimental results show an appreciably lower maximum level of PAC (viz 300 mM) produced after only 54 h, although enzyme activity was maintained at similar or higher values than in the simulation results. It is possible that the increasing PAC concentrations and associated by-products (acetoin and acetaldehyde) have resulted in significant inhibition of PDC during the course of the biotransformation and future model development will need to include one or more product inhibition terms in its structure. © 2006 Elsevier B.V. All rights reserved. |
format |
Conference or Workshop Item |
author |
Leksawasdi N. Rosche B. Rogers P. |
spellingShingle |
Leksawasdi N. Rosche B. Rogers P. Enzymatic processes for fine chemicals and pharmaceuticals: Kinetic simulation for optimal R-phenylacetylcarbinol production |
author_facet |
Leksawasdi N. Rosche B. Rogers P. |
author_sort |
Leksawasdi N. |
title |
Enzymatic processes for fine chemicals and pharmaceuticals: Kinetic simulation for optimal R-phenylacetylcarbinol production |
title_short |
Enzymatic processes for fine chemicals and pharmaceuticals: Kinetic simulation for optimal R-phenylacetylcarbinol production |
title_full |
Enzymatic processes for fine chemicals and pharmaceuticals: Kinetic simulation for optimal R-phenylacetylcarbinol production |
title_fullStr |
Enzymatic processes for fine chemicals and pharmaceuticals: Kinetic simulation for optimal R-phenylacetylcarbinol production |
title_full_unstemmed |
Enzymatic processes for fine chemicals and pharmaceuticals: Kinetic simulation for optimal R-phenylacetylcarbinol production |
title_sort |
enzymatic processes for fine chemicals and pharmaceuticals: kinetic simulation for optimal r-phenylacetylcarbinol production |
publishDate |
2014 |
url |
http://www.scopus.com/inward/record.url?eid=2-s2.0-33745783275&partnerID=40&md5=2aaf5b88099a98110e1dcd80b22ae198 http://cmuir.cmu.ac.th/handle/6653943832/570 |
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1681419507883573248 |