Propionate acts as earboxylic group acceptor in aspartate fermentation by ropionibacterium freudenreichii
| dc.contributor.author | Rosner, Bettina M. | deu |
| dc.contributor.author | Schink, Bernhard | |
| dc.date.accessioned | 2011-03-24T17:33:40Z | deu |
| dc.date.available | 2011-03-24T17:33:40Z | deu |
| dc.date.issued | 1990 | deu |
| dc.description.abstract | Cells of Propionibacterium freudenreichii ssp. shermanii and ssp. freudenreichii did not show significant growth or product formation in a mineral medium with 10 mM aspartate or 10 mM fumarate, vitamins, and a small amount (0.05% w/v) of yeast extract. In the presence of added propionate, growth with aspartate or fumarate was possible, and depended strictly on the amount of propionate provided, according to the equation: 3 aspartate + propionate ~ 3 succinate + acetate + CO2 + 3 NH3. Cocultures of P.freudenreichii with the succinate-decarboxylating strain Ft2 converted 3 aspartate stoichiometrically to acetate and 2 propionate. High activity of methylmalonyl-CoA: pyruvate transcarboxylase, and lack of methylmalonyl-CoA decarboxylase and oxaloacetate decarboxylase activity in cell-free extracts of aspartate-grown cells indicated that failure to use aspartate as sole substrate was due to the inability of these strains to catalyze a net decarboxylation of C4- dicarboxylic acids. | eng |
| dc.description.version | published | |
| dc.format.mimetype | application/pdf | deu |
| dc.identifier.citation | First publ. in: Archives of Microbiology 155 (1990), 1, pp. 46-51 | deu |
| dc.identifier.ppn | 263597253 | deu |
| dc.identifier.uri | http://kops.uni-konstanz.de/handle/123456789/7341 | |
| dc.language.iso | eng | deu |
| dc.legacy.dateIssued | 2007 | deu |
| dc.rights | Attribution-NonCommercial-NoDerivs 2.0 Generic | |
| dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/2.0/ | |
| dc.subject | Aspartate fermentation | deu |
| dc.subject | Transcarboxylase | deu |
| dc.subject | Decarboxylases | deu |
| dc.subject | Anaerobic cocultures | deu |
| dc.subject | Propionate fermentation | deu |
| dc.subject | Succinate fermentation | deu |
| dc.subject.ddc | 570 | deu |
| dc.title | Propionate acts as earboxylic group acceptor in aspartate fermentation by ropionibacterium freudenreichii | eng |
| dc.type | JOURNAL_ARTICLE | deu |
| dspace.entity.type | Publication | |
| kops.citation.bibtex | @article{Rosner1990Propi-7341,
year={1990},
title={Propionate acts as earboxylic group acceptor in aspartate fermentation by ropionibacterium freudenreichii},
number={1},
volume={155},
issn={0302-8933},
journal={Archives of Microbiology},
pages={46--51},
author={Rosner, Bettina M. and Schink, Bernhard}
} | |
| kops.citation.iso690 | ROSNER, Bettina M., Bernhard SCHINK, 1990. Propionate acts as earboxylic group acceptor in aspartate fermentation by ropionibacterium freudenreichii. In: Archives of Microbiology. 1990, 155(1), pp. 46-51. ISSN 0302-8933. eISSN 1432-072X | deu |
| kops.citation.iso690 | ROSNER, Bettina M., Bernhard SCHINK, 1990. Propionate acts as earboxylic group acceptor in aspartate fermentation by ropionibacterium freudenreichii. In: Archives of Microbiology. 1990, 155(1), pp. 46-51. ISSN 0302-8933. eISSN 1432-072X | eng |
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<dcterms:abstract xml:lang="eng">Cells of Propionibacterium freudenreichii ssp. shermanii and ssp. freudenreichii did not show significant growth or product formation in a mineral medium with 10 mM aspartate or 10 mM fumarate, vitamins, and a small amount (0.05% w/v) of yeast extract. In the presence of added propionate, growth with aspartate or fumarate was possible, and depended strictly on the amount of propionate provided, according to the equation: 3 aspartate + propionate ~ 3 succinate + acetate + CO2 + 3 NH3. Cocultures of P.freudenreichii with the succinate-decarboxylating strain Ft2 converted 3 aspartate stoichiometrically to acetate and 2 propionate. High activity of methylmalonyl-CoA: pyruvate transcarboxylase, and lack of methylmalonyl-CoA decarboxylase and oxaloacetate decarboxylase activity in cell-free extracts of aspartate-grown cells indicated that failure to use aspartate as sole substrate was due to the inability of these strains to catalyze a net decarboxylation of C4- dicarboxylic acids.</dcterms:abstract>
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