Exploiting cell metabolism for biocatalytic whole-cell transamination by recombinant Saccharomyces cerevisiae.
(2014) In Applied Microbiology and Biotechnology 98(10). p.4615-4624- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4334326
- author
- Weber, Nora LU ; Gorwa-Grauslund, Marie-Francoise LU and Carlquist, Magnus LU
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Applied Microbiology and Biotechnology
- volume
- 98
- issue
- 10
- pages
- 4615 - 4624
- publisher
- Springer
- external identifiers
-
- pmid:24557569
- wos:000335460700029
- scopus:84900832208
- pmid:24557569
- ISSN
- 1432-0614
- DOI
- 10.1007/s00253-014-5576-z
- language
- English
- LU publication?
- yes
- id
- 03f5707a-7594-46d2-9c98-fcd44cfbfbe8 (old id 4334326)
- date added to LUP
- 2016-04-01 10:10:51
- date last changed
- 2022-04-27 19:26:50
@article{03f5707a-7594-46d2-9c98-fcd44cfbfbe8, 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.}}, author = {{Weber, Nora and Gorwa-Grauslund, Marie-Francoise and Carlquist, Magnus}}, issn = {{1432-0614}}, language = {{eng}}, number = {{10}}, pages = {{4615--4624}}, publisher = {{Springer}}, series = {{Applied Microbiology and Biotechnology}}, title = {{Exploiting cell metabolism for biocatalytic whole-cell transamination by recombinant Saccharomyces cerevisiae.}}, url = {{http://dx.doi.org/10.1007/s00253-014-5576-z}}, doi = {{10.1007/s00253-014-5576-z}}, volume = {{98}}, year = {{2014}}, }