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IBEC Seminar: Emilio Parisini
viernes, marzo 22 @ 12:00 pm–1:00 pm
Engineering enzymes for biomedical and biotechnological applications
Emilio Parisini, Latvian Institute of Organic Synthesis (Riga, Latvia), University of Bologna (Italy)
Enzyme engineering has the potential to improve the activity, the stability and the substrate recognition of enzymes. As such, it paves the way for the design of novel enzymes with improved performances for a wide range of applications. This rational approach can accelerate the production and the use of biocatalysts in different biotechnological sectors, thus in turn allowing the improvement of chemical processes through the application of green chemistry concepts. In this talk, two examples from our current research will be discussed:
Fructosyl Peptide Oxidases (FPOX) are deglycating enzymes that find application as key enzymatic components in diabetes monitoring devices. Indeed, their use with blood samples can provide a measurement of the concentration of glycated hemoglobin and glycated albumin, two well-known diabetes markers. However, the FPOX currently employed in enzymatic assays cannot directly detect whole glycated proteins, making it necessary to perform a preliminary proteolytic treatment of the target protein to generate small glycated peptides that can act as viable substrates for the enzyme. This is a costly and time consuming step. The rapidly growing demand for cheap, efficient and rapid diabetes monitoring tests could be met by developing enzymatic assays for glycated hemoglobin and albumin that do not require a preliminary digestion of the proteins. In our lab, we used an in silico protein engineering approach to enhance the overall thermal stability of the enzyme and widen it active site to improve its catalytic activity toward large substrates.
The fast and uncontrolled accumulation of plastic waste in the environment has long begun to impact on the natural ecosystems and to pose an existential threat to all forms of life on our planet. Advanced technical solutions to the plastic waste management problem are therefore in urgent demand. To this end, enzymatic approaches to plastic degradation hold great promises as novel and more efficient enzymes are constantly being developed. Leaf-branch Compost Cutinase (LCC), a naturally occurring PETase, has been reported to outperform all other known PET-degrading enzymes and to present a melting temperature (Tm) of 84.7°C. This enzyme has been noticeably engineered in 2020, leading to the so-called ICCG variant (Tm = 94.0°C), the current gold standard. In our lab, we engineered a LCC that features significantly enhanced PETase activity and thermal stability relative to the gold standard ICCG.
