Premium
Experimental determination of thermodynamic equilibrium in biocatalytic transamination
Author(s) -
Tufvesson Pär,
Jensen Jacob S.,
Kroutil Wolfgang,
Woodley John M.
Publication year - 2012
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.24472
Subject(s) - transamination , equilibrium constant , chemistry , thermodynamics , chemical equilibrium , constant (computer programming) , simple (philosophy) , thermodynamic equilibrium , biochemical engineering , organic chemistry , computer science , physics , enzyme , epistemology , programming language , engineering , philosophy
The equilibrium constant is a critical parameter for making rational design choices in biocatalytic transamination for the synthesis of chiral amines. However, very few reports are available in the scientific literature determining the equilibrium constant ( K ) for the transamination of ketones. Various methods for determining (or estimating) equilibrium have previously been suggested, both experimental as well as computational (based on group contribution methods). However, none of these were found suitable for determining the equilibrium constant for the transamination of ketones. Therefore, in this communication we suggest a simple experimental methodology which we hope will stimulate more accurate determination of thermodynamic equilibria when reporting the results of transaminase‐catalyzed reactions in order to increase understanding of the relationship between substrate and product molecular structure on reaction thermodynamics. Biotechnol. Bioeng. 2012; 109:2159–2162. © 2012 Wiley Periodicals, Inc.