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Fermentation of cellodextrins by different yeast strains
P Gondé1, B Blondin, M Leclerc
1Chaire de Génétique et Microbiologie ENSA-INRA, 34060 Montpellier Cedex, France.
Applied and Environmental Microbiology
|August 1, 1984
Summary
Two yeast species, Torulopsis molischiana and T. wickerhamii, effectively ferment cellodextrins by utilizing exocellular beta-glucosidase. Other species showed limited fermentation capabilities with endocellular enzymes.
Area of Science:
- Microbiology
- Enzymology
- Biochemistry
Background:
- Cellodextrins are polymers of glucose units linked by beta-glycosidic bonds.
- Yeast species exhibit varying abilities to metabolize complex carbohydrates like cellodextrins.
- Beta-glucosidases are key enzymes in the hydrolysis of beta-glucosides.
Purpose of the Study:
- To investigate the cellodextrin fermentation capabilities of eight yeast species.
- To characterize the beta-glucosidase activity (exocellular vs. endocellular) in these yeast species.
- To determine the relationship between yeast species, enzyme location, and fermentation efficiency of cellodextrins.
Main Methods:
- Monitoring the fermentation of cellodextrins by eight selected yeast species.
- Assessing the ability of yeast to ferment beta-glucosides with varying degrees of polymerization (1-6).
- Differentiating between exocellular and endocellular beta-glucosidase activity.
Main Results:
- Only Torulopsis molischiana and T. wickerhamii fermented beta-glucosides (degree of polymerization 1-6), exhibiting exocellular beta-glucosidase activity.
- Four other yeast species fermented cellotriose (degree of polymerization 3).
- The remaining two species fermented only cellobiose (degree of polymerization 2), possessing endocellular beta-glucosidase.
Conclusions:
- Torulopsis molischiana and T. wickerhamii possess the necessary exocellular beta-glucosidase for efficient cellodextrin fermentation.
- Yeast species differ in their capacity to degrade cellodextrins, correlating with the location and specificity of their beta-glucosidase.
- The study highlights the enzymatic basis for differential carbohydrate metabolism in yeast.