The Speakers

Francesca Paradisi

Professor in Pharmaceutical chemistry, University of Bern (Switzerland)


How to make biocatalysts more efficient: reaction set-up, engineering, and scalability

Research focus:

Biocatalysis is a research filed in its own right which has shown steady progresses over the last decades, it still struggles to affirm itself as a “go to” strategy for synthetic applications in an industrial setting. In fact, while some nice examples which  involve enzymes in key steps for the production of pharmaceuticals have been developed, these are almost like white flies in the overall pool of marketed drugs and chemicals. Why is it? Does biocatalysis really stand a chance of becoming a complementary technology on large scale? In this lecture, an overview of the different steps we have taken over the last few years to bridge the gap between academia and industry will be discussed. Enzyme immobilisation, flow chemistry, engineering, and waste minimisation are at the core of our research for truly sustainable and scalable reactions.


Towards next-generation microbial cell factories - Novel biocatalysts and techniques


Research focus:

My group is working on the development of novel biocatalytic tools such as artificial metalloenzymes to endow microbes, and in particular E. coli, with capabilities that do not readily occur in nature. To achieve this, we develop and apply screening and selection methods that allow to assess large libraries of variants for different properties of interest. Further, we rely on the obtained data to develop predictive models and tools for smart library design with the goal to rationalize and thus streamline the engineering of microbial cell factories.

Markus Jeschek

Junior Group Leader, ETH Zürich (Switzerland)

Group of Prof. Sven Panke

Susana Velasco-Lozano

Post-Doctoral Researcher, CIC Biomagune (Spain)

Group of Prof. Fernando López-Gallego


Cascade biotransformations catalyzed by immobilized heterogeneous biocatalysts

Research focus:

Inspired by nature, we intend to understand the pivotal role of the ordering and compartmentalization of multi enzymatic systems participating in metabolic pathways inside living cells. To attain such goal, we develop new selective enzymatic immobilization techniques on porous matrixes. We specifically activated such materials in order to control the spatial orientation and distribution of the immobilized enzymes within the matrix-surface at the macro, micro and nano scale.


Data integration and data mining for navigation in protein sequence space.

Research focus:

We design and maintain databases on protein sequences that are enriched with both structural and experimental data.

The management of our steadily growing sequence databases is facilitated by repeatable bioinformatic workflows, with a focus on protein sequence networks.

My goal is to improve annotation and selection of candidate enzymes for experimenters interested in biocatalysis or protein evolution.

Patrick Buchholz

Post-Doctoral Researcher, University of Stuttgart (Germany)

Group of Prof. Dr. Jürgen Pleiss


Hans Iding

Laboratory Head of Roche Pharmaceuticals

Basel (Switzerland)


Enzymatic Pictet-Spengler Reactions

Stereoselective catalysts for the Pictet-Spengler reaction of tryptamines and aldehydes may allow a simple and fast approach to chiral 1-substituted tetrahydro-β-carbolines. Although biocatalysts have previously been employed for the Pictet-Spengler reaction, not a single one accepts benzaldehyde and its substituted derivatives. To address this challenge, a combination of substrate walking and transfer of beneficial mutations between different wild-type backbones was used to develop a strictosidine synthase from Rauvolfia serpentina (RsSTR) into a suitable enzyme for the asym. Pictet-Spengler condensation of tryptamine and benzaldehyde derivatives. The double variant RsSTR V176L/V208A accepted various ortho-, meta- and para-substituted benzaldehydes and produced the corresponding chiral 1-aryl-tetrahydro-β-carbolines with up to 99% enantiomeric excess.