Response surface methodology as an approach to determine the optimal activities of xylose reductase and xylitol dehydrogenase enzymes from Candida Mogii

Applied Microbiology and Biotechnology
Z D MayerhoffT T Franco

Abstract

A central composite experimental design leading to a set of 16 experiments with different combinations of pH and temperature was performed to attain the optimal activities of xylose reductase (XR) and xylitol dehydrogenase (XDH) enzymes from Candida mogii cell extract. Under optimized conditions (pH 6.5 and 38 degrees C), the XR and XDH activities were found to be 0.48 U/ml and 0.22 U/ml, respectively, resulting in an XR to XDH ratio of 2.2. Stability, cofactor specificity and kinetic parameters of the enzyme XR were also evaluated. XR activity remained stable for 3 h under 4 and 38 degrees C and for 4 months of storage at -18 degrees C. Studies on cofactor specificity showed that only NADPH-dependent XR was obtained under the cultivation conditions employed. The XR present in C. mogii extracts showed a superior Km value for xylose when compared with other yeast strains. Besides, this parameter was not modified after enzyme extraction by aqueous two-phase system.

References

Apr 26, 2000·Canadian Journal of Microbiology·K TakamizawaK Kawai
Apr 17, 2002·Applied Microbiology and Biotechnology·T Granström, M Leisola
Apr 20, 2002·Applied Biochemistry and Biotechnology·E V CortezM Vitolo
Oct 1, 1960·Nature·C CHIANG, S G KNIGHT

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