David Roura Padrosa

inSEIT AG

For the manufacture of enantiopure amines, greener synthesis processes are needed. Transaminases (TAs) are able to produce chiral amines with excellent enantioselectivity and in mild conditions, and can be immobilized to target stability, recoverability, and reusability. In the perspective of process intensification, we propose to study TA immobili...

The immobilization of copper‐containing nitrite reductase (NiR) from Alcaligenes faecalis on functionalised multi‐walled carbon nanotube (MWCNT) electrodes is reported. It is demonstrated that this immobilization is mainly driven by hydrophobic interactions, promoted by the modification of MWCNTs with adamantyl groups. Direct electrochemistry shows...

Protein bioinformatics has been applied to a myriad of opportunities in biocatalysis from enzyme engineering to enzyme discovery, but its application in enzyme immobilization is still very limited. Enzyme immobilization brings clear advantages in terms of sustainability and cost‐efficiency but is still limited in its implementation. This, because i...

To improve sustainability, safety and cost-efficiency of synthetic methodologies, biocatalysis can be a helpful ally. In this work, a novel chemoenzymatic stategy ensures the rapid synthesis of hordenine, a valuable phenolic phytochemical under mild working conditions. In a two-step cascade, the immobilized tyrosine decarboxylase from Lactobacillus...

Four pharmaceutically relevant nucleoside analogues (5-fluoro-2′-deoxyuridine, 5-chloro-2′-deoxyuridine, 5-bromo-2′-deoxyuridine, and 5-iodo-2′-deoxyuridine) have been synthesized by using a novel thymidine phosphorylase from the halotolerant H. elongata (HeTP). Following enzyme immobilization on microbeads, the biocatalyst was implemented as a pac...

The use of enzymes (protein catalysts from biological origin) has been key to the development of our society and daily life since the dawn of humanity. Nowadays, the better understanding of how enzymes work and their manipulation has enabled enzymes to become a crucial technology in the current biotechnological revolution. In this sense, while enzy...

Enzyme cascades are a powerful technology to develop environmentally friendly and cost-effective synthetic processes to manufacture drugs, as they couple different biotransformations in sequential reactions to synthesize the product. These biocatalytic tools can address two key parameters for the pharmaceutical industry: an improved selectivity of...

Did you know that the microscopic world has its own superheroes? These tiny heroes are called extremophiles. Extremophiles are microorganisms that can survive in the most dangerous places on Earth, such as hot streams or icebergs. Extremophiles can survive in these harsh environments because they have molecular tools called enzymes, which help them...

A novel fusion protein has been rationally designed, combining the hexameric glutamate dehydrogenase from Clostridium symbiosum with the dimeric formate dehydrogenase from Candida boidinii. The former enzyme consumes ammonia for the reductive amination of α-ketoglutarate using NADH, while the latter biocatalyst regenerates continuously the cofactor...

A 2-step flow-based chemo-enzymatic synthesis of selected cinnamoyl tryptamines as potential cosmetic ingredients has been developed. A first reaction catalyzed by immobilized Pd(OAc)2 gave the acyl donors employed as starting material in the second step, with very good yields (67-70%) and rapid reaction times (30 min). A second bioreactor made of...

Inspired by the boom of new artificial metalloenzymes, we developed an Fmoc-protected histidinium salt (Hum) as N-heterocyclic carbene precursor. Hum was placed via solid-phase peptide synthesis into short 7-mer peptides....

Transaminases have arisen as one of the main biocatalysts for amine production but despite their many advantages, their stability is still a concern for widespread application. One of the reasons for their instability is the need to use an excess of the amino donor when trying to synthesise amines with unfavourable equilibria. To circumvent this, r...

The integration of enzyme-catalyzed reactions in flow systems has been boosted during the last few years. Flow chemistry has been proposed in modern synthetic chemistry as a technology for process intensification. On the other hand, biocatalysis is officially recognized as a tool to increase reaction specificity and sustainability, however applicat...

Motivation: Protein immobilization, while widespread to unlock enzyme potential in biocatalysis, remains tied to a trial an error approach. Nonetheless, several databases and computational methods have been developed for protein characterization and their study. CapiPy is a user-friendly application for protein model creation and subsequent analys...

Expanding the toolbox of enzymatic reactions accessible to organic chemists is one of the major goals in biocatalysis. Here we describe the development of an acyltransferase variant from Mycobacterium smegmatis in which a strategic Ser/Cys exchange in the catalytic triad dramatically expanded its synthetic capability to yield a biocatalyst able to...

Protein immobilization while widespread to unlock enzyme potential in biocatalysis, remains tied to the trial an error approach. Nonetheless, several databases and computational methods have been applied for protein characterization and their study. CapiPy is a user-friendly application for protein model creation and subsequent analysis with specia...

Alcohol dehydrogenases (ADH) are versatile and useful enzymes employed as biocatalysts, especially for the selective oxidation of primary and secondary alcohols, and for the reduction of carbonyl moieties. A new alcohol dehydrogenase (HeADH‐II) has been identified from the genome of the halo‐adapted bacterium Halomonas elongata, which proved stable...

As an alternative to the traditional chemical synthesis or in-vivo production of L-Pipecolic acid, we have developed two ex-vivo strategies using purified and immobilised enzymes for the production of this key building block. Firstly, a transaminase capable of lysine ε-deamination was coupled with a novel pyrroline-5-carboxylate reductase, yielding...

Transaminases are pyridoxal-5'-phosphate (PLP) binding enzymes, broadly studied for their potential industrial application. Their affinity for PLP has been related to their performance and operational stability and while significant differences in PLP requirements have been reported, the environment of the PLP-binding pocket is highly conserved. In...

Hydrolytic enantioselective cleavage of different racemic non-steroidal anti-inflammatory drugs (NSAIDs) ester derivatives has been studied. An engineered esterase form Bacillus subtilis (BS2m) significantly outperformed homologous enzymes from Halomonas elongata (HeE) and Bacillus coagulants (BCE) in the enantioselective hydrolysis of naproxen est...

Ribonucleases are proteins whose use is promising in anticancer therapy. We have previously constructed different human pancreatic ribonuclease variants that are selectively cytotoxic for tumor cells by introducing a nuclear localization signal into their sequence. However, these modifications produced an important decrease in their stability compr...

Enzyme immobilisation is a common strategy to increase enzymes resistance and reusability in a variety of excellent ‘green’ applications. However, the interaction with the solid support often leads to diminished specific activity, especially when non-specific covalent binding to the carrier takes place which affects the delicate architecture of the...