Optimized oxidoreductases for medium and large scale industrial biotransformations
Total records:
126
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[ 2017 ]
Rencoret J, Pereira A, del Río JC, Martínez AT, Gutiérrez A Delignification and Saccharification Enhancement of Sugarcane Byproducts by a Laccase-Based Pretreatment
Sustainable Chem. Eng., 5: 7145-7154
[ 2017 ]
Rodríguez-Escribano D, de Salas F, Pardo I, Camarero S High-Throughput Screening Assay for Laccase Engineering toward Lignosulfonate Valorization
Int. J. Mol. Sci., 18: 1793-1803
[ 2016 ]
Acebes S, Fernandez-Fueyo E, Monza E, Lucas F, Almendral D, Ruiz-Dueñas FJ, Lund H, Martínez AT, Guallar V Rational Enzyme Engineering Through Biophysical and Biochemical Modeling
ACS-Catalysis, 6: 1624-1629
[ 2016 ]
Couturier M, Mathieu Y, Li A, Navarro D, Drula E, Haon M, Grisel S, Ludwig R, Berrin JG Characterization of a new aryl-alcohol oxidase secreted by the phytopathogenic fungus Ustilago maydis
Appl. Microbiol. Biotechnol., 100: 697-706
[ 2016 ]
de Salas F, Pardo I, Salavagione HJ, Aza P, Amourgi E, Vind J, Martínez AT, Camarero S Advanced Synthesis of Conductive Polyaniline Using Laccase as Biocatalyst
PlosOne, 11
[ 2016 ]
del Río JC, Prinsen P, Cadena EM, Martínez AT, Gutiérrez A, Rencoret J Lignin–carbohydrate complexes from sisal (Agave sisalana) and abaca (Musa textilis): chemical composition and structural modifications during the isolation process
Planta, 243: 1143-1158
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.
Official webpage of
[ 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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