Optimized oxidoreductases for medium and large scale industrial biotransformations
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126
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[ 2014 ]
Pita M, Maté D, González-Pérez D, Shleev S, Fernández VM, Alcalde M, De Lacey AL Bioelectrochemical Oxidation of Water
J. Am. Chem. Soc., 136: 5892-5895
[ 2014 ]
Piumi F, Levasseur A, Navarro D, Zhou S, Macellaro G, Mathieu Y, Ropartz D, Ludwig R, Faulds CB, Record E A novel glucose dehydrogenase from the white-rot fungus Pycnoporus cinnabarinus: production in Aspergillus niger and physicochemical characterization of the recombinant enzyme.
Appl. Microbiol. Biotechnol., 98: 10105-10118
[ 2014 ]
Rico A, Rencoret J, del Río JC, Martínez AT, Gutiérrez A Pretreatment with laccase and a phenolic mediator degrades lignin and enhances saccharification of Eucalyptus feedstock
Biotechnol. Biofuels, 7: 6
[ 2013 ]
Babot ED, del Río JC, Kalum L, Martínez AT, Gutiérrez A Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from Coprinopsis cinerea
Biotechnol. Bioeng., 110: 2323-2332
[ 2013 ]
Bey M, Zhou S, Poidevin L, Henrissat B, Coutinho PM, Berrin JG, Sigoillot JC Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) from Podospora anserina
Appl. Environ. Microbiol., 79: 488-496
[ 2013 ]
Carabajal M, Kellner H, Levin L, Jehmlich N, Hofrichter M, Ullrich R The secretome of Trametes versicolor grown on tomato juice medium and purification of the secreted oxidoreductases including a versatile peroxidase
J. Biotech., 168: 15-23
year2013
Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) from Podospora anserina
Bey M, Zhou S, Poidevin L, Henrissat B, Coutinho PM, Berrin JG, Sigoillot JC
Appl. Environ. Microbiol., 79: 488-496
The genome of the coprophilic ascomycete Podospora anserina encodes 33 different genes encoding copper-dependent lytic polysaccharide monooxygenases (LPMOs) from glycoside hydrolase family 61 (GH61). In this study, two of these enzymes (P. anserina GH61A [PaGH61A] and PaGH61B), which both harbored a family 1 carbohydrate binding module, were successfully produced in Pichia pastoris. Synergistic cooperation between PaGH61A or PaGH61B with the cellobiose dehydrogenase (CDH) of Pycnoporus cinnabarinus on cellulose resulted in the formation of oxidized and nonoxidized cello-oligosaccharides. A striking difference between PaGH61A and PaGH61B was observed through the identification of the products, among which were doubly and triply oxidized cellodextrins, which were released only by the combination of PaGH61B with CDH. The mass spectrometry fragmentation patterns of these oxidized products could be consistent with oxidation at the C-6 position with a geminal diol group. The different properties of PaGH61A and PaGH61B and their effect on the interaction with CDH are discussed in regard to the proposed in vivo function of the CDH/GH61 enzyme system in oxidative cellulose hydrolysis.
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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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