Improved conversion of methanol to single-cell protein by Methylophilus methylotrophus

Improved conversion of methanol to single-cell protein by Methylophilus methylotrophus

The glutamate dehydrogenase gene of Escherichia coli has been cloned into broad host-range plasmids and can complement glutamate synthase mutants of Methylophilus methylotrophus. Assimilation of ammonia via glutamate dehydrogenase is more energy-efficient than via glutamate synthase, thus the recomb...

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Veröffentlicht in:Nature (London) 1980-10, Vol.287 (5781), p.396-401
Hauptverfasser: Windass, J. D., Worsey, M. J., Pioli, E. M., Pioli, D., Barth, P. T., Atherton, K. T., Dart, E. C., Byrom, D., Powell, K., Senior, P. J.
Format: Artikel
Sprache:eng
Schlagworte:
Adenosine Triphosphate - metabolism
Ammonia - metabolism
Bacterial Proteins - biosynthesis
DNA, Recombinant
Escherichia coli - enzymology
Genetic Engineering - methods
Glutamate Dehydrogenase - genetics
Glutamate Synthase - metabolism
Humanities and Social Sciences
Methanol - metabolism
Methylococcaceae - enzymology
Methylococcaceae - metabolism
multidisciplinary
Plasmids
Science
Science (multidisciplinary)
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Zusammenfassung:The glutamate dehydrogenase gene of Escherichia coli has been cloned into broad host-range plasmids and can complement glutamate synthase mutants of Methylophilus methylotrophus. Assimilation of ammonia via glutamate dehydrogenase is more energy-efficient than via glutamate synthase, thus the recombinant organism converts more growth substrate, methanol, into cellular carbon.
ISSN:0028-0836
1476-4687
DOI:10.1038/287396a0