Anne S. Meyer
Head of Protein Chemistry & Enzyme Technology, DTU Bioengineering
Anne S. Meyer is Professor of Enzyme Technology and Head of the Protein Chemistry & Enzyme Technology Division at the DTU Department of Biotechnology and Biomedicine. She holds an MSc from the University of Copenhagen, an MSc from the University of Reading, UK, and a PhD from DTU. Anne has been employed at DTU since 1988 in various positions, and had two postdoc stays in the USA at University California Davis. She became Full Professor at DTU in 2006 and headed the Center for BioProcess Engineering at DTU until summer 2018, when she assumed her current role. From 2017 to 2020, Anne was a visiting professor at the Department Chemical and Biomolecular Engineering, University of Melbourne, Australia.
3 questions to Anne S. Meyer
What do you appreciate most about working at your university and/or your department?
What I really like about working at the Technical University of Denmark, DTU, is the spirit. At DTU the spirit is that everybody wants to make a difference. Incredibly, everybody thus believes in the vision that the whole idea is “to develop and create value using the natural sciences and the technical sciences to benefit society”! This vision is the original foundation of the University formulated almost 200 years ago by the founder of the University, H.C. Ørsted – he also happened to be the father of electromagnetism. It is a powerful vision, and it sets a strong direction and provides a very meaningful cause for the work, both the research and the teaching. Although this vision does sound a bit loud and ponderous, it is a driver.
At my Department, DTU Bioengineering, we specifically work with biotechnology, and I particularly work with enzyme proteins. The research work is all about engineering the molecules of life, and the real fascination for me lies in the process of learning and understanding how nature works. For me it is the “detective work” that is deeply fascinating, and I have to confess that I particularly find it interesting to work with research questions and processes that have a direct relation to usefulness in practical application.
The field of enzyme technology that I work within is also the subject of my teaching – and I teach courses on “Enzyme Technology and Kinetics” and “Experimental Enzyme Technology” – most of the course content is about enzyme kinetics, but the course names emphasizing technology seem more appealing to students! While I do like to teach, I really mostly appreciate the daily research work, ranging from discovery of new enzymes, over detailed resolution of how the enzymes work, to imagining new processes in which the particular enzymatic catalysis can help. The whole research concept and raison d’être of this field of research is to create new ideas and options for solving a problem or pursue a new opportunity – typically obtaining a new product or find new enzyme for removal or recycling of specific compounds.
Which topic could you talk about for hours?
I can talk for hours about a lot of things and a lot of topics. Overall, I spend a lot of time on considering new ideas, and I literally do spend time every day to discuss how enzymes work. Hence, when considering how enzymatic catalysis can be used in new processes and products several topics are key, that I can illustrate with some examples:
1) In the EuroPostdoc2 project “CO2FDH-21” that I am involved in supervising, held by Liliana Calzadiaz-Ramirez here at DTU Bioengineering, it is all about investigating and developing enzymes for CO2 conversion. It is important to understand that genuine enzyme catalyzed CO2 conversion to a new chemical compound such as formic acid HCOOH (or formate, HCOO-) is different from the enzyme catalyzed CO2 solubilization reaction that converts CO2 and water to bicarbonate and a proton. The latter reaction is catalyzed by carbonic anhydrase and is use to maintain the pH balance in living organisms. In contrast, the specific enzyme catalyzed CO2 conversion to formic acid, catalyzed by formate dehydrogenase activity (FDH), is the reaction that we can use to actually produce new chemicals from CO2. Although formic acid is a consolidated commodity chemical, the concept becomes more interesting if you consider formic acid as a feedstock for green synthesis to substitute a range of petrochemicals, including methanol. Hence, in this way, FDH catalyzed conversion of CO2 becomes an option for both reducing CO2 emissions and simultaneously providing for a new supply route of current high-in-demand chemicals.
2) Another point is that most natural enzymes are not designed to be robust enough for our use. The key point is therefore to understand in detail how the enzymes work, which structural features that determine robustness such as thermal stability, robustness at alternative pH values etc., and then engineer the enzymes to fit the process requirements. This is an amazing and important part of the research we do.
3) I also work with other types of reactions targeting the new bioeconomy. These include upcycling of various natural plant biomass and seaweed substrates and even plastics. In these reactions the enzymes have to act on an insoluble substrate. First, we still don’t always understand how the catalytic function of enzyme proteins actually works to accelerate the chemical reaction, second, the way and the kinetics speed of these enzyme reactions usually differ from classic Michaelis-Menten kinetics.
So to make many long stories short, what I can talk about for hours is how we constantly have to expand the fundamental knowledge (in my case of how enzymes work) in order to use biocatalysis in new processes.
What project or endeavour are you looking forward to?
I look very much forward to working closely with Liliana on her EuroTech postdoc project concerning discovery and development of robust enzymes for CO2 conversion. Apart from the subject area being immensely interesting and meaningful, the built-in aspect of collaboration with university partners in the 5 tech circle is a really nice aspect. This project is co-supervised by Professor Xile Hu from Laboratory of Inorganic Synthesis and Catalysis, Ecole Polytechnique Fédérale de Lausanne (EPFL). Professor Hu has expertise in electrochemical CO2 reduction that fits extremely well to support Liliana’s research. In addition, the project also involves collaboration with Asst. Prof. Omer Yehezkeli from Technion Israel, as his knowledge and lab-set up regarding bioelectrochemistry applications is super interesting and can help advance the technical set-up of the FDH catalyzed CO2 conversion in practice. So I really look forward to this project.
