The Â鶹AV Protein and Peptide Group is organising the "Early Career Seminars on Peptide and Protein Science" series. This virtual seminar series highlights the latest developments in peptide and protein science, reaching a diverse audience that includes peptide and protein chemists, carbohydrate chemists, and chemical biologists.
In December 2024, the early career researchers presenting will be
Dr Alex Brogan
Senior Lecturer in Chemistry
King's College London
https://www.kcl.ac.uk/people/alex-brogan
Title: Expanding the scope of enzyme biocatalysis through chemical modification and ionic liquids
Abstract: Enzymes can perform many industrially relevant reactions, such as esterification, hydrolysis, oxidation, reduction, and C-C bond formation, with high specificity and under significantly milder conditions than their chemical counterparts. As a result, research into the use of enzymes as industrial biocatalysts has been gaining ground, particularly in conjunction with emerging solvent systems such as ionic liquids. However, enzymes often have very low solubilities in nonaqueous environments and are frequently unstable, limiting the window of usability. Consequently, there is a need to develop new biotechnologies that improve solubility and stability of biocatalysts in nonaqueous media.
Chemical modification of enzyme surfaces has been demonstrated as a robust method for stabilizing enzymes against temperature, aggregation, and non-aqueous environments. Recent work showed that modified enzymes are soluble in both hydrophilic and hydrophobic ionic liquids, with biomolecule structure preserved in the non-aqueous environment. Using the enzyme glucosidase it was demonstrated that in ionic liquids, the optimal temperature shifted to 110 °C, which was accompanied by a 30-fold enhancement of the enzyme activity as well as reactivity towards water insoluble cellulose. Here, ongoing work stabilizing a range of enzymes in ionic liquids and deep eutectic solvents will be presented. In particular, work on developing new biocatalytic strategies for broad-spectrum plastic recycling, as well as process intensification of biofuel production, will be highlighted. Overall, this talk will demonstrate of how protein-stabilization, in conjunction with emerging solvent systems, could provide a versatile platform technology for broadening the substrate scope of industrial biocatalysis.
Dr Mateo Isidro Sanchez Lopez
Wellcome Trust Fellow
University of Cambridge
https://www.ch.cam.ac.uk/person/mis40
Title: Protease engineering for applications in neuroscience and cell biology
Abstract: Proteases are one of the most used enzymes in cell biology and biotechnological applications. Viral plant proteases, such as TEV (for Tobacco etch virus protease), form the core of many molecular tools such as scFLARE or FLiCRE due to their exquisite sequence specificity and orthogonality to the mammalian proteome. These systems transform transient neuronal activity into long-lasting outputs such as the expression of a reporter gene, and are leveraged for the mapping and manipulation of active neuronal circuits underlying specific behaviours.
In this talk, in addition to explaining the molecular mechanisms of these tools and our recent efforts to increase their performance, we will also discuss ongoing projects in protease engineering to trigger biological events such as the engineering of gas vesicles to produce ultrasound imaging in response to enzymatic activity.
Date: 06/12/2024
Time: 1:00-2:00 pm
Venue: online Zoom seminars
For upcoming series, please visit the Â鶹AV PPSG website.
If you would like to present in future seminars, please contact one of the organisers.
Lucia Lombardi: l.lombardi@imperial.ac.uk
Rachel Dickman: rachael.dickman.13@ucl.ac.uk
Louis Luk: lukly@cardiff.ac.uk
In December 2024, the early career researchers presenting will be
Dr Alex Brogan
Senior Lecturer in Chemistry
King's College London
https://www.kcl.ac.uk/people/alex-brogan
Title: Expanding the scope of enzyme biocatalysis through chemical modification and ionic liquids
Abstract: Enzymes can perform many industrially relevant reactions, such as esterification, hydrolysis, oxidation, reduction, and C-C bond formation, with high specificity and under significantly milder conditions than their chemical counterparts. As a result, research into the use of enzymes as industrial biocatalysts has been gaining ground, particularly in conjunction with emerging solvent systems such as ionic liquids. However, enzymes often have very low solubilities in nonaqueous environments and are frequently unstable, limiting the window of usability. Consequently, there is a need to develop new biotechnologies that improve solubility and stability of biocatalysts in nonaqueous media.
Chemical modification of enzyme surfaces has been demonstrated as a robust method for stabilizing enzymes against temperature, aggregation, and non-aqueous environments. Recent work showed that modified enzymes are soluble in both hydrophilic and hydrophobic ionic liquids, with biomolecule structure preserved in the non-aqueous environment. Using the enzyme glucosidase it was demonstrated that in ionic liquids, the optimal temperature shifted to 110 °C, which was accompanied by a 30-fold enhancement of the enzyme activity as well as reactivity towards water insoluble cellulose. Here, ongoing work stabilizing a range of enzymes in ionic liquids and deep eutectic solvents will be presented. In particular, work on developing new biocatalytic strategies for broad-spectrum plastic recycling, as well as process intensification of biofuel production, will be highlighted. Overall, this talk will demonstrate of how protein-stabilization, in conjunction with emerging solvent systems, could provide a versatile platform technology for broadening the substrate scope of industrial biocatalysis.
Dr Mateo Isidro Sanchez Lopez
Wellcome Trust Fellow
University of Cambridge
https://www.ch.cam.ac.uk/person/mis40
Title: Protease engineering for applications in neuroscience and cell biology
Abstract: Proteases are one of the most used enzymes in cell biology and biotechnological applications. Viral plant proteases, such as TEV (for Tobacco etch virus protease), form the core of many molecular tools such as scFLARE or FLiCRE due to their exquisite sequence specificity and orthogonality to the mammalian proteome. These systems transform transient neuronal activity into long-lasting outputs such as the expression of a reporter gene, and are leveraged for the mapping and manipulation of active neuronal circuits underlying specific behaviours.
In this talk, in addition to explaining the molecular mechanisms of these tools and our recent efforts to increase their performance, we will also discuss ongoing projects in protease engineering to trigger biological events such as the engineering of gas vesicles to produce ultrasound imaging in response to enzymatic activity.
Date: 06/12/2024
Time: 1:00-2:00 pm
Venue: online Zoom seminars
For upcoming series, please visit the Â鶹AV PPSG website.
If you would like to present in future seminars, please contact one of the organisers.
Lucia Lombardi: l.lombardi@imperial.ac.uk
Rachel Dickman: rachael.dickman.13@ucl.ac.uk
Louis Luk: lukly@cardiff.ac.uk
