Proteins with putative erythrose reductase activity have been identified in the filamentous fungiTrichoderma reesei,ÿAspergillus niger,ÿandÿFusarium graminearumÿby in silico analysis. The proteins found inÿT. reeseiÿandÿA. nigerÿhad earlier been characterized as glycerol dehydrogenase and aldehyde reductase, respectively. Corresponding genes from all three fungi were cloned, heterologously expressed inÿEscherichia coli,ÿand purified. Subsequently, they were used to establish optimal enzyme assay conditions. All three enzymes strictly require NADPH as cofactor, whereas with NADH no activity could be observed. The enzymatic characterization of the three enzymes using ten substrates revealed high substrate specificity and activity with D-erythrose and D-threose. The enzymes fromÿT. reeseiÿandÿA. nigerÿherein showed comparable activities, whereas the one fromÿF. graminearumÿreached only about a tenth of it for all tested substrates. In order to proof in vivo the proposed enzyme function, we overexpressed the erythrose reductase-encoding gene inÿT. reesei.ÿAn increased production of erythritol by the recombinant strain compared to the parental strain could be detected.

Author Name: Birgit Jovanovi?, Robert L Mach, Astrid R Mach-Aigner

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Keywords: 21910855,Characterization of erythrose reductases from filamentous fungi,21910855,Birgit Jovanovi?, Robert L Mach, Astrid R Mach-Aigner

ISSN: 21910855

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