Explore the words cloud of the OXIDISE project. It provides you a very rough idea of what is the project "OXIDISE" about.
The following table provides information about the project.
UNIVERSITAET FUER BODENKULTUR WIEN
|Coordinator Country||Austria [AT]|
|Total cost||1˙929˙319 €|
|EC max contribution||1˙929˙319 € (100%)|
1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
|Duration (year-month-day)||from 2017-03-01 to 2022-02-28|
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|1||UNIVERSITAET FUER BODENKULTUR WIEN||AT (WIEN)||coordinator||1˙929˙319.00|
Current processes for lignocellulose deconstruction are unspecific and produce some constituents in poor quality. Specific biocatalysts could achieve optimal segregation together with minimal damage to cellulose and lignin and provide high-quality feedstocks for industry. Naturally occurring fungal oxidoreductases perform this task, but their characterisation – and hence their optimisation for industrial application – is difficult because of the experimental challenges. The mission of OXIDISE to develop appropriate methods to characterise lignocellulose degrading oxidoreductases, i.e. elucidate their conversions rates and to resolve their distribution and interaction in vicinity of their polymeric substrates. High-resolution techniques will be adapted to specifically detect fungal oxidoreductases like lytic polysaccharide monooxygenase, cellobiose dehydrogenase, laccase, lignin peroxidase, or members of the GMC oxidoreductase superfamily. These enzymes are all involved in the oxidative attack of recalcitrant biopolymers and are present in over 90% of fungal genomes. To overcome problems of current assaying techniques such as their low spatial and temporal resolution, OXIDISE will develop and apply techniques based on microelectrodes, scanning electron microscopy, surface plasmon resonance and fluorescence microscopy thereby pursuing three objectives: 1) study the interaction of all major oxidoreductases secreted by fungi in regard to electron transfer, regeneration of redox species and substrate cascading; 2) resolve the distribution of secreted oxidoreductases on cellulosic and lignocellulosic substrates at high resolution; 3) transfer the developed techniques to natural lignocellulose samples with growing fungal hyphae and study the secreted oxidoreductase activities. OXIDISE strives to establish new techniques to elucidate the kinetics and interactions of oxidoreductases – a long neglected enzyme class for lignocellulose depolymerisation.
|year||authors and title||journal||last update|
Jani Tuoriniemi, Lo Gorton, Roland Ludwig, Gulnara Safina
Determination of the Distance Between the Cytochrome and Dehydrogenase Domains of Immobilized Cellobiose Dehydrogenase by Using Surface Plasmon Resonance with a Center of Mass Based Model
published pages: 2620-2627, ISSN: 0003-2700, DOI: 10.1021/acs.analchem.9b04490
|Analytical Chemistry 92/3||2020-04-01|
Annabelle T. Abrera, Hucheng Chang, Daniel Kracher, Roland Ludwig, Dietmar Haltrich
Characterization of pyranose oxidase variants for bioelectrocatalytic applications
published pages: 140335, ISSN: 1570-9639, DOI: 10.1016/j.bbapap.2019.140335
|Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1868/2||2020-04-01|
Stefan Scheiblbrandner, Roland Ludwig
Cellobiose dehydrogenase: Bioelectrochemical insights and applications
published pages: 107345, ISSN: 1567-5394, DOI: 10.1016/j.bioelechem.2019.107345
Su Ma, Christophe V. F. P. Laurent, Marta Meneghello, Jani Tuoriniemi, Chris Oostenbrink, Lo Gorton, Philip N. Bartlett, Roland Ludwig
Direct Electron-Transfer Anisotropy of a Site-Specifically Immobilized Cellobiose Dehydrogenase
published pages: 7607-7615, ISSN: 2155-5435, DOI: 10.1021/acscatal.9b02014
|ACS Catalysis 9/8||2019-10-03|
Marta Meneghello, Firas A. Alâ€Lolage, Su Ma, Roland Ludwig, Philip N. Bartlett
Studying Direct Electron Transfer by Siteâ€Directed Immobilization of Cellobiose Dehydrogenase
published pages: 700-713, ISSN: 2196-0216, DOI: 10.1002/celc.201801503
Su Ma, Roland Ludwig
Direct Electron Transfer of Enzymes Facilitated by Cytochromes
published pages: 958-975, ISSN: 2196-0216, DOI: 10.1002/celc.201801256
Leander SÃ¼tzl, Christophe V. F. P. Laurent, Annabelle T. Abrera, Georg SchÃ¼tz, Roland Ludwig, Dietmar Haltrich
Multiplicity of enzymatic functions in the CAZy AA3 family
published pages: 2477-2492, ISSN: 0175-7598, DOI: 10.1007/s00253-018-8784-0
|Applied Microbiology and Biotechnology 102/6||2019-05-29|
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