NADH-linked aldose reductase: the key to anaerobic alcoholic fermentation of xylose by yeasts View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1984-04

AUTHORS

Peter M. Bruinenberg, Peter H. M. de Bot, Johannes P. van Dijken, W. Alexander Scheffers

ABSTRACT

The kinetics and enzymology of d-xylose utilization were studied in aerobic and anaerobic batch cultures of the facultatively fermentative yeasts Candida utilis, Pachysolen tannophilus, and Pichia stipitis. These yeasts did not produce ethanol under aerobic conditions. When shifted to anaerobiosis cultures of C. utilis did not show fermentation of xylose; in Pa. tannophilus a very low rate of ethanol formation was apparent, whereas with Pi. stipitis rapid fermentation of xylose occurred. The different behaviour of these yeasts ist most probably explained by differences in the nature of the initial steps of xylose metabolism: in C. utilis xylose is metabolized via an NADPH-dependent xylose reductase and an NAD+-linked xylitol dehydrogenase. As a consequence, conversion of xylose to ethanol by C. utilis leads to an overproduction of NADH which blocks metabolic activity in the absence of oxygen. In Pa. tannophilus and Pi. stipitis, however, apart from an NADPH-linked xylose reductase also an NADH-linked xylose reductase was present. Apparently xylose metabolism via the NADH-dependent reductase circumvents the imbalance of the NAD+/NADH redox system, thus allowing fermentation of xylose to ethanol under anaerobic conditions. The finding that the rate of xylose fermentation in Pa. tannophilus and Pi. stipitis corresponds with the activity of the NADH-linked xylose reductase activity is in line with this hypothesis. Furthermore, a comparative study with various xylose-assimilating yeasts showed that significant alcoholic fermentation of xylose only occurred in those organisms which possessed NADH-linked aldose reductase. More... »

PAGES

256-260

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00251847

DOI

http://dx.doi.org/10.1007/bf00251847

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1028456095


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