Effect of growth conditions on cofactor linked xylose reductase activity in pachysolen tannophilus

Vancauwenberge, J.E.; Bolen, P.L.; Mccracken, D.A.; Bothast, R.J.

Enzyme and Microbial Technology 11(10): 662-667


ISSN/ISBN: 0141-0229
DOI: 10.1016/0141-0229(89)90005-7
Accession: 007248887

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Xylose reductase (E.C. is the enzyme responsible for conversion of xylose to xylitol in the fermentation of pentoses to ethanol by the yeast P. tannophilus. Cell-free extracts from anaerobically grown cells yield two forms of xylose reductase. One form requires either NADPH or NADH as a cofactor and has an isoelectric point (pI) of 5.1. A second from requires only NADPH as a cofactor and has a pI of 6.4. Cell-free extracts from aerobically grown cells also yielded two reductase forms, but the NADPH-active form predominated. Both forms have a molecular weight of 36,000 daltons. These two forms exhibiting xylose reductase activity may exist as two separate proteins or possibly as a single protein that undergoes modification.