Optimized oxidoreductases for medium and large scale industrial biotransformations
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Dr Marta Pérez-Boada
E-mail: MPBoada@cib.csic.es
Consejo Superior de Investigaciones Científicas (CSIC)
Biological Research Centre (CIB)
Calle Ramiro de Maeztu 9, E-28040 Madrid, Spain
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publications
Total records: 126
Pages:    1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21  

[ 2014 ] González-Pérez D, Molina-Espeja P, García-Ruiz E, Alcalde M Mutagenic Organized Recombination Process by Homologous In vivo Grouping (MORPHING) for directed enzyme evolution PlosOne, 9: 3
[ 2014 ] Hofrichter M, Ullrich R Oxidations catalyzed by fungal peroxygenases Curr. Opin. Chem. Biol., 19: 116-125
[ 2014 ] Hori C, [...] , Ferreira P, Ruiz-Dueñas FJ, [...] , Rencoret J, Gutiérrez A, [...] , Martínez AT, [...] , Cullen D Analysis of the Phlebiopsis gigantea Genome, Transcriptome and Secretome Provides Insight into Its Pioneer Colonization Strategies of Wood PLOS Genetics, 10: 1004759
[ 2014 ] Isaksen T, Westereng B, Aachmann FL, Agger JW, Kracher D, Kittl R, Ludwig R, Haltrich D, Eijsink VG, Horn SJ A C4-oxidizing lytic polysaccharide monooxygenase cleaving both cellulose and cello-oligosaccharides J. Biol. Chem., 289: 2632-2642
[ 2014 ] Kalum L, Morant MD, Lund H, Jensen J, Lapainaite I, Soerensen NH, Pedersen S, Ostergaard LH, Xu F Enzymatic oxidation of 5-hydroxymethylfurfural and derivatives thereof. WO 2014015256 A2. International Patent Application
[ 2014 ] Kellner H, Luis P, Pecyna MJ, Barbi F, Kapturska D, Krüger D, Zak DR, Marmeisse R, Vandenbol M, Hofrichter M Widespread Occurrence of Expressed Fungal Secretory Peroxidases in Forest Soils PlosOne, 9
year2014
Effective mutations in a high redox potential laccase from Pleurotus ostreatus
Macellaro G, Baratto MC, Piscitelli A, Pezzella C, Fabrizi de Biani F, Palmese A, Piumi F, Record E, Basosi R, Sannia G
Appl. Microbiol. Biotechnol., doi: 10.1007/s00253-013-5491-8

Since the first report on a laccase, there has been a notable development in the interest towards this class of enzymes, highlighted from the number of scientific papers and patents about them. At the same time, interest in exploiting laccases—mainly high redox potential—for various functions has been growing exponentially over the last 10 years. Despite decades of work, the molecular determinants of the redox potential are far to be fully understood. For this reason, interest in tuning laccase redox potential to provide more efficient catalysts has been growing since the last years. The work herein described takes advantage of the filamentous fungus Aspergillus niger as host for the heterologous production of the high redox potential laccase POXA1b from Pleurotus ostreatus and of one of its in vitro selected variants (1H6C). The system herein developed allowed to obtain a production level of 35,000 U/L (583.3 μkat/L) for POXA1b and 60,000 U/L (1,000 μkat/L) for 1H6C, corresponding to 13 and 20 mg/L for POXA1b and 1H6C, respectively. The characterised proteins exhibit very similar characteristics, with some exceptions regarding catalytic behaviour, stability and spectro-electrochemical properties. Remarkably, the 1H6C variant shows a higher redox potential with respect to POXA1b. Furthermore, the spectro-electrochemical results obtained for 1H6C make it tempting to claim that we spectro-electrochemically determined the redox potential of the 1H6C T2 site, which has not been studied in any detail by spectro-electrochemistry yet.

Official webpage of indox [ 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 garcíarincón