BIFI TALK: Ariadna Pié Porta, Department of Chemical and Biochemical Engineering, Technical University of Denmark

Title:Oxidases and their Michaels Constant for Oxygen: Relevance and Measurement

Abstract

Medicine has benefited from the great features of enzymes for many years. During the past decades, the interest in the application of enzymes as (bio)catalysts to produce a wide range of valuable compounds has increased. In particular, oxidative reactions are crucial in many synthetic processes for the production of a wide range of chemicals. Oxidative biocatalysis has a number of pros and cons regarding the need of a constant supply of oxygen, which affect kinetics and stability. Often, oxidative biocatalytic processes tend to become oxygen limited. Not only oxygen is a rather hydrophobic molecule (the maximum concentration of oxygen dissolved in water in equilibrium with air is 250 µM), but also industrially-relevant enzymes tend to have a rather high Michaelis constant for oxygen (K_MO). This is, considering oxygen a secondary substrate in the reaction, enzymes reach only low reaction rates even at the maximum concentration of dissolved oxygen in the media. On one hand, oxygen limitation reduces the rate of the reaction in an industrial perspective, and on the other hand, prevents scientists from measuring and calculating the correct and absolute KM for any oxygen-related enzyme that does not reach its maximum rate of reaction. To address this issue, we present the Tube-in-Tube Reactor Setup¹. The Tube-in-Tube Reactor Setup is a novel tool that allows the saturation of virtually any enzyme with oxygen in order to determine its absolute K_MO.

References: Ringborg, R. H.; Toftgaard Pedersen, A.; Woodley, J. M. Automated Determination of Oxygen-Dependent Enzyme Kinetics in a Tube-in-Tube Flow Reactor. ChemCatChem 2017, 9 (17), 3285–3288. https://doi.org/10.1002/cctc.201700811.

FRIDAY, 22 November 2024, 12:30 h
Sala de grados Grados de la Facultad de Ciencias (edificio A)