Elia Calderini

ORCID: 0000-0003-3991-6182
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About
Contact & Profiles
Research Areas
  • Enzyme Catalysis and Immobilization
  • Microbial Metabolic Engineering and Bioproduction
  • Plant biochemistry and biosynthesis
  • Biochemical and biochemical processes
  • Metal-Catalyzed Oxygenation Mechanisms
  • Microbial bioremediation and biosurfactants
  • Protein Hydrolysis and Bioactive Peptides
  • Probiotics and Fermented Foods
  • Photosynthetic Processes and Mechanisms
  • Asymmetric Synthesis and Catalysis
  • Photochromic and Fluorescence Chemistry
  • Axial and Atropisomeric Chirality Synthesis
  • Chemical synthesis and alkaloids
  • Enzyme Structure and Function
  • Biochemical Analysis and Sensing Techniques

Graz University of Technology
2020-2024

Institute of Molecular Biotechnology
2020-2024

Technische Universität Braunschweig
2019-2021

Technical University of Denmark
2017

Light-dependent enzymes are a rare type of biocatalyst with high potential for research and biotechnology. A recently discovered fatty acid photo-decarboxylase from Chlorella variabilis NC64A (CvFAP) converts acids to the corresponding hydrocarbons only when irradiated blue light (400 520 nm). To expand available catalytic diversity decarboxylation, we reconstructed possible ancestral decarboxylases set 12 extant sequences that were classified under clade within glucose-methanol choline...

10.1002/cbic.202000851 article EN cc-by ChemBioChem 2021-02-05

Probiotic cultures encounter oxidative conditions during manufacturing, yet protein abundance changes induced by such stress have not been characterized for some of the most common probiotics and starters. This comparative proteomics investigation focuses on response Lactobacillus acidophilus NCFM to H2 O2, simulating an environment. Bacterial growth was monitored BioScreen batch were harvested at exponential phase profiling responses 2D gel based proteomics. Proteins identified in 19 21...

10.1002/pmic.201600178 article EN PROTEOMICS 2017-01-03

Abstract Halohydrin dehalogenases (HHDHs) are valuable biocatalysts for the synthesis of β‐substituted alcohols based on their epoxide ring‐opening activity with a number small anionic nucleophiles. In an attempt to further broaden scope substrates accepted by these enzymes, panel 22 HHDHs was investigated in conversion aliphatic and aromatic vicinally di‐substituted trans ‐epoxides using azide as nucleophile. The majority able convert methyl‐substituted corresponding azidoalcohols, some...

10.1002/cctc.201900103 article EN cc-by-nc-nd ChemCatChem 2019-02-28

Enzymatic decarboxylation of biobased hydroxycinnamic acids gives access to phenolic styrenes for adhesive production. Phenolic acid decarboxylases are proficient enzymes that have been applied in aqueous systems, organic solvents, biphasic and deep eutectic which makes stability a key feature. Stabilization the enzyme would increase total turnover number thus reduce energy consumption waste accumulation associated with biocatalyst In this study, we used ancestral sequence reconstruction...

10.1021/acssuschemeng.3c06513 article EN cc-by ACS Sustainable Chemistry & Engineering 2024-02-21

The development of sustainable processes for the valorization byproducts and other waste streams remains an ongoing challenge in field catalysis. Racemic borneol, isoborneol camphor are currently produced from α-pinene, a side product production cellulose. pure enantiomers these monoterpenoids have numerous applications cosmetics act as reagents asymmetric synthesis, making enzymatic route their separation into optically desirable goal. Known short-chain borneol-type dehydrogenases (BDHs)...

10.1002/cctc.202100110 article EN cc-by ChemCatChem 2021-02-12

Fe(II)- and α-ketoglutarate dependent dioxygenases have emerged as important catalysts for the preparation of non-natural amino acids. The stoichiometric supply cosubstrate (αKG) is an cost factor. A combination N-succinyl acid hydroxylase SadA with l-glutamate oxidase (LGOX) allowed coupling in situ production αKG to stereoselective αKG-dependent a one-pot/two-step cascade reaction. Both enzymes were used immobilized tested preparative scale setup under process-near conditions. Oxygen...

10.1021/acssuschemeng.0c01122 article EN cc-by ACS Sustainable Chemistry & Engineering 2020-05-13

Racemic camphor and isoborneol are readily available as industrial side products, whereas (1R)-camphor is from natural sources. Optically pure (1S)-camphor, however, much more difficult to obtain. The synthesis of racemic α-pinene proceeds via an intermediary isobornyl ester, which then hydrolyzed oxidized give camphor. We reasoned that enantioselective hydrolysis esters would facile access optically isomers, respectively. While screening a set commercial lipases esterases in the kinetic...

10.1002/cbic.202100187 article EN cc-by ChemBioChem 2021-05-25

Multi-step cascade reactions have gained increasing attention in the biocatalysis field recent years. In particular, multi-enzymatic cascades can achieve high molecular complexity without workup of reaction intermediates thanks to enzymes’ intrinsic selectivity; and where enzymes fall short, organo- or metal catalysts further expand range possible synthetic routes. Here, we present two enantiocomplementary (chemo)-enzymatic composed either a styrene monooxygenase (StyAB) Shi epoxidation...

10.3390/catal11080982 article EN Catalysts 2021-08-17
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