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Enzyme engineering

Research topics/Enzyme engineering

Naturally occurring enzymes can be modified and adapted to carry out their biocatalytic function in extreme environments or on different substrates. Such modifications often results in higher reaction yields, improved reaction specificities and enhanced enzyme stabilities under specific operational conditions. Countless experimental approaches and enzymes from different natural sources provide unlimited opportunities for basic and applied research.

Selected publications

  • Estiri H, Bhattacharya S, Rodriguez Buitrago JA, Castagna R, Legzdiņa L, Casucci G, Ricci A, Parisini E, Gautieri A. Tailoring FPOX Enzymes for Enhanced Stability and Expanded Substrate Recognition. Sci. Rep. 2023, 13, 18610. DOI: 10.1038/s41598-023-45428-1

  • Gautieri A, Rigoldi F, Torretta A, Redaelli A, Parisini E. In silico engineering of enzyme access tunnels. In: “Enzyme Engineering” – book series “Methods in Molecular Biology” (2021), Springer (Ed. Magnani F, Marabelli C, Paradisi F), ISBN 978-1-0716-1826-4

  • Rigoldi F, Donini S, Torretta A, Carbone A, Redaelli A, Bandiera T, Parisini E, Gautieri A. Rational backbone redesign of a Fructosyl Peptide Oxidase to widen its active site access tunnel. Biotechnol. Bioeng. 2020, 117, 3688. (cover article)

  • Rigoldi F, Donini S, Giacomina F, Sorana F, Redaelli A, Bandiera T, Parisini E, Gautieri A. Thermal stabilization of the deglycating enzyme Amadoriase I by rational design. Sci. Rep. 2018, 8, 3042.

  • Rigoldi F, Donini S, Redaelli A, Parisini E, Gautieri A. Engineering of Thermostable Enzymes for Industrial applications. APL Bioeng., 2018, 2, 011501. (cover article)

  • Rigoldi F, Spero L, Dalle Vedove A, Redaelli A, Parisini E, Gautieri A. Molecular dynamics simulations provide insights into the substrate specificity of FAOX family members. Mol. Biosyst., 2016, 12, 2622.

  • Rigoldi F, Gautieri A, Dalle Vedove A, Lucarelli AP, Vesentini S, Parisini E. Crystal structure of the deglycating enzyme Amadoriase I in its free form and substrate-bound complex. Proteins, 2016, 84, 744. (cover article)