Opendata, web and dolomites

OXIDISE SIGNED

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

Total Cost €

0

EC-Contrib. €

0

Partnership

0

Views

0

 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.

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

Project "OXIDISE" data sheet

The following table provides information about the project.

Coordinator
UNIVERSITAET FUER BODENKULTUR WIEN 

Organization address
address: GREGOR MENDEL STRASSE 33
city: WIEN
postcode: 1180
website: www.boku.ac.at

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

 Partnership

Take a look of project's partnership.

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

Map

 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.

 Publications

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

Are you the coordinator (or a participant) of this project? Plaese send me more information about the "OXIDISE" project.

For instance: the website url (it has not provided by EU-opendata yet), the logo, a more detailed description of the project (in plain text as a rtf file or a word file), some pictures (as picture files, not embedded into any word file), twitter account, linkedin page, etc.

Send me an  email (fabio@fabiodisconzi.com) and I put them in your project's page as son as possible.

Thanks. And then put a link of this page into your project's website.

The information about "OXIDISE" are provided by the European Opendata Portal: CORDIS opendata.

More projects from the same programme (H2020-EU.1.1.)

CHIPTRANSFORM (2018)

On-chip optical communication with transformation optics

Read More  

CUSTOMER (2019)

Customizable Embedded Real-Time Systems: Challenges and Key Techniques

Read More  

CARBYNE (2020)

New carbon reactivity rules for molecular editing

Read More