Increased pyruvate efficiency in enzymatic production of (R)-phenylacetylcarbinol |
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Authors: | Rosche Bettina Breuer Michael Hauer Bernhard Rogers Peter L |
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Institution: | (1) School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW, 2052, Australia |
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Abstract: | Loss of substrate, pyruvate, a limitation for enzymatic batch production of (R)-phenylacetylcarbinol (PAC), resulted from two phenomena: temperature dependent non-enzymatic concentration decrease due to the cofactor Mg2+ and formation of by-products, acetaldehyde and acetoin, by pyruvate decarboxylase (PDC). In the absence of enzyme, pyruvate stabilization was achieved by lowering the Mg2+ concentration from 20 to 0.5 mM. With 0.5 mM Mg2+
Rhizopus javanicus and Candida utilis PDC produced similar levels of PAC (49 and 51 g l–1, respectively) in 21 h at 6 °C; however C. utilis PDC formed less by-product from pyruvate and was more stable during biotransformation. The process enhancements regarding Mg2+ concentration and source of PDC resulted in an increase of molar yield (PAC/consumed pyruvate) from 59% (R. javanicus PDC, 20 mM Mg2+) to 74% (R. javanicus PDC, 0.5 mM Mg2+) to 89% (C. utilis PDC, 0.5 mM Mg2+). |
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Keywords: | biotransformation Candida utilis (R)-phenylacetylcarbinol pyruvate decarboxylase Rhizopus javanicus |
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