FEMS Microbiology Letters Poster Prize: Christina Pentari
We send our congratulations to Christina Pentari, who won a poster prize at the FEMS Conference on Microbiology. This award is sponsored by our journal FEMS Microbiology Letters.
The FEMS Conference on Microbiology (#FCOM22) took place on the 30th June until the 2nd July in Belgrade, Serbia. With 450 posters on display the FEMS Microbiology Letters editorial board selected Christina’s poster on a novel acetyl esterase from Thermothelomyces thermophilus as the best poster.
Read our interview with Christina about her research below:
What is your current position, and what was your scientific journey to get there?
Currently I am a PhD candidate in the field of Industrial Biotechnology at the School of Chemical Engineering of the National Technical University of Athens. I obtained my Diploma in Chemical Engineering in 2018, after I completed my Thesis on the investigation of the enzymatic lignocellulolytic system of the white rot Basidiomycete Pleurotus citrinopileatus and its biodegradation potential. Since then, I am a member of the IndBioCat group under the supervision of Assistant Prof. Evangelos Topakas. My research is mainly focused on the discovery and exploitation of biocatalysts that target recalcitrant structures of the hemicellulosic part of plant biomass. The biodegradation of hemicellulose facilitates the utilization of cellulose and thus glucose, which is the major fermentative molecule of sugar-based biorefineries. My work is funded by the HFRI foundation, as part of a research project aiming at the enzymatic valorization of Greek lignocellulosic biomass.”
Could you describe the research your poster covered?
The work presented by our team at the FEMS conference, refers to the discovery, the biochemical characterization as well as the elucidation of the crystal structure of an acetyl esterase of the carbohydrate esterase family 16 from Thermothelomyces thermophilus. The TtCE16 esterase exhibited limited sequence similarity to already characterized CE16 enzymes and was found to deacetylate xylooligosaccharides, mono- or di-acetylated, removing even the 4-O-acetyl group of the non-reducing end xylopyranose residue. The esterase displayed complementary activity to previously known esterases, leading to complete deacetylation of native acetylated xylan. In addition, the supplementation of xylanases of different glycoside hydrolase families with TtCE16, led to the enhancement of their catalytic activity on lignocellulosic biomass.
Finally, our structural studies led to the first crystal structure of a CE16 family member. This work highlights the unique specific activity of TtCE16 towards acetylated xylan and raises questions regarding its exact biological role within the microbial lignocellulolytic system. These findings lead us one step closer to the complete mapping of the enzymatic mechanisms employed by fungi for the degradation of the hemicellulose component of plant biomass.”
What do you hope to focus your research on in the future?
Hopefully, our future work will be focused on the identification of the structural determinants that promote the substrate binding within the catalytic site of TtCE16, in order to gain understanding regarding its structure-function relationship. Another goal is the utilization of TtCE16 for the degradation of recalcitrant structures of heavily substituted xylan, by investigating of its synergistic relationships with other auxiliary and main-chain xylan-degrading enzymes. Subsequently, we aim to harness the individual properties of these novel enzymes for the design of new enzymatic cocktails targeting the efficient bioconversion of lignocellulosic biomass to value-added chemicals.”
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