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Cosubstrate effect on xylose reductase and xylitol dehydrogenase activity levels, and its consequence on xylitol production by Candida tropicalis by Elena Tamburini; Ercolina Bianchini; Alessandro Bruni; Giuseppe Forlani is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Cosubstrate effect on xylose reductase and xylitol dehydrogenase activity levels, and its consequence on xylitol production by Candida tropicalis about?

Due to its anticariogenic properties, the five-carbon sugar alcohol xylitol is finding increasing use in food industry as a functional sweetener. Although xylitol is currently manufactured by the chemical reduction of xylose, its biological production would be attractive because of lower costs and better organoleptic features. In xylose-fermenting yeasts, the substrate is directly converted to xylitol by an NAD(P)H-dependent reductase (XR). Xylitol is oxidized in turn by an NAD + -dependent dehydrogenase (XDH) yielding xylulose, which is channelled into the pentose phosphate pathway. In the absence of other carbon sources, a significant fraction of xylitol is used to fuel cell growth. To avoid excess yield loss and maximize xylitol production, a series of mono-and disaccharides were tested as cosubstrates for a hyper-acidophilic strain of Candida tropicalis. Their effect upon XR and XDH specific activity levels was evaluated, and the resulting expression of the inducible pathway and the XR:XDH ratio were related to either non-optimized or optimized yields. Glucose strongly inhibited xylose reduction, whereas galactose stimulated xylitol utilization. On the contrary, the addition of

Who reads Cosubstrate effect on xylose reductase and xylitol dehydrogenase activity levels, and its consequence on xylitol production by Candida tropicalis?

It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.

Author
Elena Tamburini; Ercolina Bianchini; Alessandro Bruni; Giuseppe Forlani
Publisher
Elsevier Science; Elsevier ; Elsevier BV (ISSN 0141-0229)
Published
2010
Language
EN
Field
Biochemistry, Genetics and Molecular Biology (Life Sciences)

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