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)
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publications
Total records: 126
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[ 2013 ] Salvachúa D, Martínez AT, Tien M, López-Lucendo MF, García F, de los Ríos V, Martínez MJ, Prieto A Differential proteomic analysis of the secretome of Irpex lacteus and other white-rot fungi during wheat straw pretreatment Biotechnol. Biofuels, 6: 115-129
[ 2013 ] Salvachúa D, Prieto A, Mattinen ML, Tamminen T, Liitiä T, Lille M, Willför S, Martínez AT, Martínez MJ, Faulds CB Versatile peroxidase as a valuable tool for generating new biomolecules by homogeneous and heterogeneous cross-linking Enz. Microb. Technol., 52: 303-311
[ 2013 ] Strittmatter E, Liers C, Ullrich R, Wachter S, Hofrichter M, Plattner D, Piontek K First Crystal Structure of a Fungal High-Redox Potential Dye-decolorizing Peroxidase: Substrate Interaction Sites and Long-Range Electron Transfer J. Biol. Chem., 288: 4095-4102
[ 2013 ] Strittmatter E, Wachter S, Liers C, Ullrich R, Hofrichter M, Plattner D, Piontek K Radical formation on a conserved tyrosine residue is crucial for DyP activity Arch. Biochem. Biophys., 537: 161-167
[ 2013 ] Turbe-Doan A, Arfi Y, Record E, Estrada-Alvarado I, Levasseur A Heterologous production of cellobiose dehydrogenases from the basidiomycete Coprinopsis cinerea and the ascomycete Podospora anserina and their effect on saccharification of wheat straw Appl. Microbiol. Biotechnol., 97: 4873-4885
[ 2013 ] Wang X, Peter S, Ullrich R, Hofrichter M, Groves JT Driving Force for Oxygen-Atom Transfer by Heme-Thiolate Enzymes Angew. Chem. Int. Ed., 52: 9238-9241
year2013
Versatile peroxidase as a valuable tool for generating new biomolecules by homogeneous and heterogeneous cross-linking
Salvachúa D, Prieto A, Mattinen ML, Tamminen T, Liitiä T, Lille M, Willför S, Martínez AT, Martínez MJ, Faulds CB
Enz. Microb. Technol., 52: 303-311
The modification and generation of new biomolecules intended to give higher molecular-mass species for biotechnological purposes, can be achieved by enzymatic cross-linking. The versatile peroxidase (VP) from Pleurotus eryngii is a high redox-potential enzyme with oxidative activity on a wide variety of substrates. In this study, VP was successfully used to catalyze the polymerization of low molecular mass compounds, such as lignans and peptides, as well as larger macromolecules, such as protein and complex polysaccharides. Different analytical, spectroscopic, and rheological techniques were used to determine structural changes and/or variations of the physicochemical properties of the reaction products. The lignans secoisolariciresinol and hydroxymatairesinol were condensed by VP forming up to 8 unit polymers in the presence of organic co-solvents and Mn(2+). Moreover, 11 unit of the peptides YIGSR and VYV were homogeneously cross-linked. The heterogeneous cross-linking of one unit of the peptide YIGSR and several lignan units was also achieved. VP could also induce gelation of feruloylated arabinoxylan and the polymerization of β-casein. These results demonstrate the efficacy of VP to catalyze homo- and hetero-condensation reactions, and reveal its potential exploitation for polymerizing different types of compounds.
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