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38 2 New Trends in the In Situ Enzymatic Recycling of NAD(P)(H) Cofactors
systems to be used in ADH-catalyzed oxidations. Already established methods,
such as the pyruvate/LDH system, are sufficiently efficient and robust for industrial
applications, but the cost of the co-substrate can render them not yet sufficiently
competitive to traditional chemical oxidation methods. However, it can been
foreseen that the exploitation of O -based biocatalysts, such as NADH oxidases
2
and laccases (via redox mediator), will further boost the application of NAD(P)H-
dependent dehydrogenases toward the foreseeable development of selective and
green catalytic oxidation methods.
Acknowledgments
The authors thank the ESF project COST CM0701 for support.
References
1. Monti, D., Ottolina, G., Carrea, G., and 7. Yamamoto, H., Mitsuhashi, K., Kimoto,
Riva, S. (2011) Redox reactions catalyzed N., Kobayashi, Y., and Esaki, N. (2005)
by isolated enzymes. Chem. Rev., 111, Robust NADH-regenerator: improved
4111–4140. alpha-haloketone-resistant formate dehy-
2. Weckbecker, A., Gr¨ oger, H., and drogenase. Appl. Microbiol. Biotechnol.,
Hummel, W. (2010) in Advances in 67, 33–39.
Biochemical Engineering Biotechnology, 8. Slusarczyk, H., Felber, S., Kula, M.-R.,
vol. 120 (eds C. Wittmann and R. Krull), and Pohl, M. (2003) Novel mutants
Springer-Verlag, Berlin, Heidelberg, pp. of formate dehydrogenase from Can-
195–242. dida boidinii. US Patent Application
3. Wu, H., Tian, C., Song, X., Liu, Publication US2003/0157664, Sep. 21,
C., Yang, D., and Jiang, Z. (2013) 2003.
Methods for the regeneration of nicoti- 9. Alekseeva, A.A., Serenko, A.A., Kargov,
namide coenzymes. Green Chem., 15, I.S., Savin, S.S., Kleymenov, S.U., and
1773–1789. Tishkov, V.I. (2012) Engineering cat-
4. Tishkov, V.I. and Popov, V.O. (2006) alytic properties and thermal stability of
Protein engineering of formate dehydro- plant formate dehydrogenase by single-
genase. Biomol. Eng., 23, 89–110. point mutations. Prot.Eng.Des.Sel., 25,
5. Tishkov, V.I., Galkin, A.G., Marchenko, 781–788.
G.N., Egorova, O.A., Sheluho, D.V., 10. Tishkov, V.I., Yasnyi, I.E., Sadykhov,
Kulakova, L.B., Dementieva, L.A., and E.G., Matorin, A.D., and Serov, A.E.
Egorov, A.M. (1993) Catalytic properties (2006) Study of thermal stability of
+
and stability of a Pseudomonas sp. 101 mutant NADP -dependent formate
formate dehydrogenase mutants con- dehydrogenases from Pseudomonas
taining Cys-255-Ser and Cys-255-Met sp. 101. Dokl. Biochem. Biophys., 409,
replacements. Biochem. Biophys. Res. 216–218.
Commun., 192, 976–981. 11. Andreadeli, A., Platis, D., Tishkov, V.I.,
6. Slusarczyk, H., Felber, S., Kula, M.R., Popov, V.O., and Labrou, N.E. (2008)
and Pohl, M. (2000) Stabilization of Structure-guided alteration of coenzyme
NAD-dependent formate dehydrogenase specificity of formate dehydrogenase
from Candida boidinii by site-directed by saturation mutagenesis to enable
+
mutagenesis of cysteine residues. Eur. J. efficient utilization of NADP . FEBS J.,
Biochem., 267, 1280–1289. 275, 3859–3869.