Optimized oxidoreductases for medium and large scale industrial biotransformations
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126
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[ 2015 ]
Poraj-Kobielska M, Peter S, Leonhardt S, Ullrich R, Scheibner K, Hofrichter M Immobilization of unspecific peroxygenases (EC 1.11.2.1) in PVA/PEG gel and hollow fiber modules
Biochem. Eng. J., 98: 144-150
[ 2015 ]
Rico A, Rencoret J, del Río JC, Martínez AT, Gutiérrez A In-Depth 2D NMR Study of Lignin Modification During Pretreatment of Eucalyptus Wood with Laccase and Mediators
Bioenerg. Res., 8: 211-230
[ 2015 ]
Saez-Jimenez V, Acebes S, Guallar V, Martínez AT, Ruiz-Dueñas FJ Improving the oxidative stability of a high redox potential fungal peroxidase by rational design
PlosOne, 10-4
[ 2015 ]
Saez-Jimenez V, Baratto MC, Pogni R, Rencoret J, Gutiérrez A, Santos JI, Martínez AT, Ruiz-Dueñas FJ Demonstration of Lignin-to-Peroxidase Direct Electron Transfer: A Transient-state Kinetics, Directed Mutagenesis, EPR and NMR Study
J. Biol. Chem., 290: 23201-23213
[ 2015 ]
Saez-Jimenez V, Fernandez-Fueyo E, Medrano FJ, Romero A, Martínez AT, Ruiz-Dueñas FJ Improving the pH-stability of Versatile Peroxidase by Comparative Structural Analysis with a Naturally-Stable Manganese Peroxidase
PlosOne, doi: 10.1371/journal.pone.0140984
[ 2015 ]
Tan TC, Kracher D, Gandini R, Sygmund C, Kittl R, Haltrich D, Hällberg BM, Ludwig R, Divine C Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation
Nat. Commun., 6: 7542
year2015
Immobilization of unspecific peroxygenases (EC 1.11.2.1) in PVA/PEG gel and hollow fiber modules
Poraj-Kobielska M, Peter S, Leonhardt S, Ullrich R, Scheibner K, Hofrichter M
Biochem. Eng. J., 98: 144-150
The immobilization of enzymes has many advantages, such as higher stability, easier handling, and reuse of the catalyst. Here we report, for the first time, two effective methods for the immobilization of unspecific peroxygenase (UPO; EC 1.11.2.1). This biocatalyst type comprises heavily glycosylated heme-thiolate proteins that catalyze various biotechnologically relevant oxyfunctionalizations. Both the encapsulation in cryogel and the retention of the enzyme in hollow fiber modules were found to be efficient methods for their immobilization. After encapsulation, the enzyme still exhibited 60% of its initial activity. Interestingly, we did not find differences in the kinetic parameters of free and immobilized UPOs. In long-term experiments, the conversion of the pharmaceutical diclofenac with immobilized UPOs in different reactor types yielded between 62 mg and 154 mg of the major human drug metabolite 4′-hydroxydiclofenac. The maximal total turnover number was about 60-fold higher compared to the free enzyme. A test over 5 months showed that storage of encapsulated UPOs in non-polar solvents (e.g., cyclohexane) helps to preserve the enzyme stability and increases their relative activity (by about ∼150%, in the case of diclofenac hydroxylation). In addition to the hydrophilic substrate diclofenac, encapsulated UPOs also oxidized the hydrophobic model compound cyclohexane.
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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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