Optimized oxidoreductases for medium and large scale industrial biotransformations
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[ 2016 ]
Ewing TA, Gygli G, van Berkel WJ A single loop is essential for the octamerisation of vanillyl alcohol oxidase
FEBS J., doi: 10.1111/febs.13762
[ 2016 ]
Fernandez-Fueyo E, Ni Y, Gomez Baraibar A, Alcalde M, van Langen LM, Hollmann F Towards preparative peroxygenase-catalyzed oxyfunctionalization reactions in organic media
J. Mol. Cat. B, doi: 10.1016/j.molcatb.2016.09.013
[ 2016 ]
Fernandez-Fueyo E, Ruiz-Dueñas FJ, López-Lucendo MF, Pérez-Boada M, Rencoret J, Gutiérrez A, Pisabarro AG, Ramírez L, Martínez AT A secretomic view of woody and nonwoody lignocellulose degradation by Pleurotus ostreatus
Biotechnol. Biofuels, 9: 49
[ 2016 ]
Fernandez-Fueyo E, Younes SHH, van Rootselaar S, Aben RWM, Renirie R, Wever R, Holtmann D, Rutjes FPJT, Hollmann F A Biocatalytic Aza-Achmatowicz Reaction
ACS-Catalysis, 6: 5904-5907
[ 2016 ]
Garajova S, Mathieu Y, Beccia MR, Bennati-Granier C, Biaso F, Fanuel M, Ropartz D, Guigliarelli B, Record E, Rogniaux H, Henrissat B, Berrin JG Single-domain flavoenzymes trigger lytic polysaccharide monooxygenases for oxidative degradation of cellulose
Sci. Rep., 6: 28276
[ 2016 ]
González-Pérez D, Mateljak I, García-Ruiz E, Ruiz-Dueñas FJ, Martínez AT, Alcalde M Alkaline versatile peroxidase by directed evolution
Catal. Sci. Technol., 6: 6625-6636
year2016
Alkaline versatile peroxidase by directed evolution
González-Pérez D, Mateljak I, García-Ruiz E, Ruiz-Dueñas FJ, Martínez AT, Alcalde M
Catal. Sci. Technol., 6: 6625-6636
Ligninolytic peroxidases are involved in natural wood decay in strict acid environments. Despite their biotechnological interest, these high-redox potential enzymes are not functional at basic pH due to the loss of calcium ions that affects their structural integrity. In this study, we have built catalytic activity at basic pH in a versatile peroxidase (VP) previously engineered for thermostability. By using laboratory evolution and hybrid approaches, we designed an active and highly stable alkaline VP while the catalytic bases behind the alkaline activation were unveiled. A stabilizing mutational backbone allowed the pentacoordinated heme state to be maintained, and the new alkaline mutations hyperactivated the enzyme after incubation at basic pHs. The final mutant oxidises substrates at alkaline pHs both at the heme channel and at the Mn2+ site, while the catalytic tryptophan was not operational under these conditions. Mutations identified in this work could be transferred to other ligninolytic peroxidases for alkaline activation.
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[ industrialoxidoreductases ]. Optimized oxidoreductases for medium and large scale industrial biotransformations. This project has received funding from the European Union’s Seventh Framework Programme for research, technological development and demonstration under Grant Agreement nº: FP7-KBBE-2013-7-613549. © indox 2013. Developed by
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