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Research
Our research focuses on understanding and developing nature-inspired multi-enzyme systems, to create more sustainable and cost-effective biocatalysts and protein-based biomaterials for biomedical and biotechnological applications.
"The best is yet to come..."
Discovery of extremotolerant enzymes
Life on Earth has demonstrated incredible flexibility in thriving within the most severe conditions, from encompassing polar regions, to radioactive waste sites. Yet, only a tiny fraction of the molecular basis behind the extraordinary abilities of extremotolerant organisms is known.
We study enzymes from extremotolerant organisms as robust biocatalysts that can withstand harsh reaction conditions such as extreme pH, high temperature, or organic co-solvents to develop more efficient and greener processes.
Enzyme immobilization
The attachement of enzymes to (or entrapment into) a solid support is known as immobilization. This process not only can make enzymes more stable, but also allows the reusability of the immobilized biocatalyst. Thus, immobilized enzymes can be integrated into continuous flow reactors maximizing their cost-efficiency and productivity.
We are interested in the development of novel immobilization techniques and more eco-friendly support materials to reduce waste production.
Intrinsically disordered proteins (IDPs)
Disorder refers to the lack of a fixed 3D structure in proteins. More than 50% of the human proteome are intrinsically disordered proteins (IDPs) or proteins containing disordered regions (IDPRs). Therefore, they are fundamental biomolecules for life. However, IDPs have been typically studied in association with their role in diseases (e.g. Alzheimer).
Our goal is to harness the potential of the dynamic and unique IDPs for biotechnological purposes.
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