Energy substrate efficiency during batch cultures of Geotrich urn can didurn
Metabolisation of carbon and nitrogen substrates is a key factor during the ripening process of white soft cheeses but has not previously been examined in terms of energy substrate efficiency. Such work could be useful to improve physiological knowledge concerning Geotrichum candidum, a yeast involv...
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Veröffentlicht in: | Journal of the science of food and agriculture 2008-04, Vol.88 (6), p.984 |
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Sprache: | eng |
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Zusammenfassung: | Metabolisation of carbon and nitrogen substrates is a key factor during the ripening process of white soft cheeses but has not previously been examined in terms of energy substrate efficiency. Such work could be useful to improve physiological knowledge concerning Geotrichum candidum, a yeast involved in the neutralisation of curd during ripening. Its behaviour was therefore examined during batch cultures on simple (glutamate) or complex (peptones) substrates as nitrogen and carbon sources and lactate as a second carbon source. In addition to their assimilation as carbon and nitrogen sources, 6. candidum used peptides and amino acids as energy sources during growth in preference to lactate. Contrarily, during stationary state, lactate was preferred over peptides and amino acids for carbon dissimilation for energy supply, allowing the avoidance of ammonium production. Indeed, lactate dissimilation theoretically yields 15 adenosine triphosphates (ATPs), while only nine ATPs are theoretically yielded during the dissimilation of an amino acid such as glutamate. This behaviour can be considered as an energy-saving response. Indeed, the use of peptides and amino acids as energy sources in addition to being used as carbon and nitrogen sources during 6. candidum growth can be related to its deaminating activity and was in agreement with the better energy efficiency expected from utilisation of the same substrate as both carbon and energy source. Contrarily, the better efficiency of lactate dissimilation led to its use during stationary state instead of peptides and amino acids. |
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ISSN: | 0022-5142 1097-0010 |