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Background   Pichia stipitis  xylose reductase (Ps-XR) has been used to design  Saccharomyces cerevisiae  strains that are able to ferment xylose. One example is the industrial  S. cerevisiae  xylose-consuming strain TMB3400, which was constructed by expression of  P. stipitis  xylose reductase and xylitol dehydrogenase and overexpression of endogenous xylulose kinase in the industrial  S. cerevisiae  strain USM21.    Results  In this study, we demonstrate that strain TMB3400 not only converts xylose, but also displays higher tolerance to lignocellulosic hydrolysate during anaerobic batch fermentation as well as 3 times higher  in vitro  HMF and furfural reduction activity than the control strain USM21. Using laboratory strains producing various levels of Ps-XR, we confirm that Ps-XR is able to reduce HMF both  in vitro  and  in vivo . Ps-XR overexpression increases the  in vivo  HMF conversion rate by approximately 20%, thereby improving yeast tolerance towards HMF. Further purification of Ps-XR shows that HMF is a substrate inhibitor of the enzyme.    Conclusion  We demonstrate for the first time that xylose reductase is also able to reduce the furaldehyde compounds that are present in undetoxified lignocellulosic hydrolysates. Possible implications of this newly characterized activity of Ps-XR on lignocellulosic hydrolysate fermentation are discussed.

Pichia stipitis xylose reductase helps detoxifying lignocellulosic hydrolysate by reducing 5-hydroxymethyl-furfural (HMF)