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Interaction and Kinetics of Oxidative Biomass Degrading Enzymes Resolved by High-Resolution Techniques

Total Cost €


EC-Contrib. €






 OXIDISE project word cloud

Explore the words cloud of the OXIDISE project. It provides you a very rough idea of what is the project "OXIDISE" about.

oxidoreductase    enzymes    regard    members    techniques    polymeric    resonance    microelectrodes    appropriate    laccase    current    genomes    interactions    mission    regeneration    cellulose    substrates    interaction    transfer    fungi    lignocellulosic    oxidative    samples    electron    fungal    species    industrial    depolymerisation    constituents    industry    scanning    segregation    cellulosic    strives    difficult    rates    90    characterise    secreted    feedstocks    poor    class    kinetics    minimal    biopolymers    assaying    optimal    degrading    recalcitrant    naturally    unspecific    quality    experimental    oxidise    elucidate    damage    oxidoreductases    polysaccharide    occurring    vicinity    substrate    microscopy    lignocellulose    characterisation    spatial    cellobiose    pursuing    overcome    perform    monooxygenase    dehydrogenase    detect    cascading    biocatalysts    thereby    lytic    surface    optimisation    enzyme    plasmon    fluorescence    deconstruction    superfamily    resolution    conversions    resolve    attack    redox    hence    temporal    gmc    natural    peroxidase    hyphae    lignin   

Project "OXIDISE" data sheet

The following table provides information about the project.


Organization address
city: WIEN
postcode: 1180

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Austria [AT]
 Total cost 1˙929˙319 €
 EC max contribution 1˙929˙319 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2016-COG
 Funding Scheme ERC-COG
 Starting year 2017
 Duration (year-month-day) from 2017-03-01   to  2022-02-28


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    UNIVERSITAET FUER BODENKULTUR WIEN AT (WIEN) coordinator 1˙929˙319.00


 Project objective

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
List of publications.
2020 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
2020 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
2020 Stefan Scheiblbrandner, Roland Ludwig
Cellobiose dehydrogenase: Bioelectrochemical insights and applications
published pages: 107345, ISSN: 1567-5394, DOI: 10.1016/j.bioelechem.2019.107345
Bioelectrochemistry 131 2019-10-03
2019 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
2018 Marta Meneghello, Firas A. Al‐Lolage, Su Ma, Roland Ludwig, Philip N. Bartlett
Studying Direct Electron Transfer by Site‐Directed Immobilization of Cellobiose Dehydrogenase
published pages: 700-713, ISSN: 2196-0216, DOI: 10.1002/celc.201801503
ChemElectroChem 6/3 2019-10-03
2019 Su Ma, Roland Ludwig
Direct Electron Transfer of Enzymes Facilitated by Cytochromes
published pages: 958-975, ISSN: 2196-0216, DOI: 10.1002/celc.201801256
ChemElectroChem 6/4 2019-10-03
2018 Leander Sützl, Christophe V. F. P. Laurent, Annabelle T. Abrera, Georg Schütz, 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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