|
type |
Journal Article |
authors |
Weber N, Gorwa-Grauslund M, Carlquist M. |
title |
Exploiting cell metabolism for biocatalytic whole-cell transamination by recombinant Saccharomyces cerevisiae |
journal |
Appl Microbiol Biotechnol |
Activity |
2.6.1.96 |
Family |
2.6.1.96 |
sel |
selected |
ui |
24557569 |
year |
(2014) |
volume |
98 |
number |
10 |
pages |
4615-24 |
| |
keywords |
doi: 10.1007/s00253-014-5576-z. |
abstract |
The potential of Saccharomyces cerevisiae for biocatalytic whole-cell transamination was investigated using the kinetic resolution of racemic 1-phenylethylamine (1-PEA) to (R)-1-PEA as a model reaction. As native yeast do not possess any ω-transaminase activity for the reaction, a recombinant yeast biocatalyst was constructed by overexpressing the gene coding for vanillin aminotransferase from Capsicum chinense. The yeast-based biocatalyst could use glucose as the sole co-substrate for the supply of amine acceptor via cell metabolism. In addition, the biocatalyst was functional without addition of the co-factor pyridoxal-5′-phosphate (PLP), which can be explained by a high inherent cellular capacity to sustain PLP-dependent reactions in living cells. In contrast, external PLP supplementation was required when cell viability was low, as it was the case when using pyruvate as a co-substrate. Overall, the results indicate a potential for engineered S. cerevisiae as a biocatalyst for whole-cell transamination and with glucose as the only co-substrate for the supply of amine acceptor and PLP. |
last changed |
2019/01/08 09:22 |
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