Organisation/Company IFP Energies nouvelles (IFPEN) Research Field Chemistry » Biochemistry Researcher Profile Established Researcher (R3) Positions Postdoc Positions Country France Application Deadline 31 Mar 2025 - 23:00 (Europe/Brussels) Type of Contract Temporary Job Status Full-time Hours Per Week 35 Offer Starting Date 15 Jan 2025 Is the job funded through the EU Research Framework Programme? Not funded by a EU programme Is the Job related to staff position within a Research Infrastructure? No
Offer Description The current postdoc position at IFPEN is for one year starting in Octobre 2024.
Scientific environment:
IFP Energies nouvelles (IFPEN) is a major research and training player in the fields of energy, transport and the environment. From scientific concepts within the framework of fundamental research, through to technological solutions in the context of applied research, innovation is central to its activities, hinged around four strategic directions: climate, environment and circular economy – renewable energies – sustainable mobility – responsible oil and gas.
As part of the public-interest mission with which it has been tasked by the public authorities, IFPEN focuses its efforts on bringing solutions to the challenges facing society and industry in terms of energy and the climate, to support the ecological transition. An integral part of IFPEN, IFP School, its graduate engineering school, prepares future generations to take up these challenges.
The Biotechnology department at IFPEN Rueil-Malmaison is composed of dynamic and young research teams working on biofuels (bioethanol) and biobased chemicals. The applicant will integrate the biochemistry team that is working on cellulases.
Research project:
Lytic Polysaccharide Monooxygenases (LPMOs) are well-studied monocopper enzymes known for their "boosting effect" on the enzymatic hydrolysis of recalcitrant polysaccharides such as chitin [1] and cellulose [2]. In nature, LPMOs play a pivotal role in the global carbon cycle during biomass decay. These enzymes have a great biotechnological interest and are important component of industrial enzyme cocktails used to produce bioproducts (e.g. bioethanol) from lignocellulosic biomass [3]. However, LPMOs functionality is far from being completely understood [4]. The large diversity of LPMOs is today represented by their distribution in eight auxiliary activity (AA9-AA11; AA13-AA17) families of the CAZy database [5].
The postdoc candidate will express and purify several previously uncharacterized and atypical LPMO enzymes in flask and bioreactors, and then determine their biochemical parameters. He/She will define the best implementation conditions to maximize the deconstruction of lignocellulosic biomass in synergy with purified enzymes or enzymatic cocktails. This postdoctoral research project is part of the ANR-funded SNOEBORD project (21-CE43-0025 ). The candidate will work in the biotechnology department of IFPEN at Rueil Malmaison and collaborate with Bastien Bissaro and Jean-Guy Berrin from the laboratory " B iodiversité & B iotechnologie F ongique" at INRAE Marseille.
Expected profile of the candidate:
A PhD obtained recently (less than 3 year) with theoretical and practical knowledge in biochemistry and enzymology with skills in expression and purification of recombinant proteins. Background in lignocellulosic biomass conversion and bioprocesses will be appreciated. The candidate should have good communication skills in English for oral presentation and scientific writing. Communication skills in French are a plus but not mandatory.
[1] Vaaje-Kolstad G, et al.(2010) An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science.
330(6001): p. 219-22.
[2] Quinlan RJ, et al. (2011) Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass
[3] Rosso, MN, Berrin JG, and Lomascolo A (2022) Plant wastes and sustainable refineries: What can we learn from fungi? CurrentOpinion in Green and Sustainable Chemistry. 34: p. 100602.
[4] Vandhana TM, et al. (2022) On the expansion of biological functions of lytic polysaccharide monooxygenases. New Phytol. 233(6):
p. 2380-2396.
[5] Drula E, et al. (2022) The carbohydrate-active enzyme database: functions and literature. Nucleic Acids Res. 50(D1): p. D571-D577.
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