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Total records: 126
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[ 2013 ] Churakova E, Arends IWCE, Hollmann F Increasing the Productivity of Peroxidase-Catalyzed Oxyfunctionalization: A Case Study on the Potential of Two-Liquid-Phase Systems ChemCatChem, 5: 565-568

[ 2013 ] Hahn F, Ullrich R, Hofrichter M, Liers C Experimental approach to follow the spatiotemporal wood degradation in fungal microcosms Biotechnol. J., 8: 127-132

[ 2013 ] Karich A, Kluge M, Ullrich R, Hofrichter M Benzene oxygenation and oxidation by the peroxygenase of Agrocybe aegerita AMB Express, 3: 5-13

[ 2013 ] Kluge M, Ullrich R, Scheibner K, Hofrichter M Formation of naphthalene hydrates in the enzymatic conversion of 1,2-dihydronaphthalene by two fungal peroxygenases and subsequent naphthalene formation J. Mol. Cat. B, doi: 10.1016/j.molcatb.2013.08.017

[ 2013 ] Liers C, Aranda E, Strittmatter E, Piontek K, Plattner D, Zorn H, Ullrich R, Hofrichter M Phenol oxidation by DyP-type peroxidases in comparison to fungal and plant peroxidases J. Mol. Cat. B, doi: 10.1016/j.molcatb.2013.09.025

[ 2013 ] Liers C, Pecyna MJ, Kellner H, Worrich A, Zorn H, Steffen KT, Hofrichter M, Ullrich R Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases Appl. Microbiol. Biotechnol., 97: 5839-5849

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.