Mangiagalli Marco, PhD
Assistant Professor of Biochemistry
room 5054, building U3, tel.: +39 02 6448 3518
lab 5014, building U3, tel. +39 02 6448 3523
Orcid , Web of Science ResearcherIDQ-9988-2018 , Scopus Author ID: 57192680227 , Google Scholar , Linkedin
The activity is focused on the following research lines
Industrial Biotechnology
Protein engineering, Molecular modelling and structural biology
Enviromental Biodiversity and Ecosystem
Microbial Diversity and Bioprospecting
Keywords
Biocatalysis, Biophysical techniques, Cold-active enzymes, Enzyme discovery, Glycoside hydrolases, Ice Binding Proteins, Protein structure, Recombinant protein production.
Background
Marco Mangiagalli graduated cum laude in industrial biotechnology at the University of Milano Bicocca and received in 2019 a PhD in Biology and Biotechnology at the University of Milano Bicocca. Since 2022 he is assistant professor at the Department of Biotechnology and Biosciences of the University of Milano Bicocca. His scientific interests focus on understanding the function-structure relationship of cold-active enzymes and the effects of organic solvents on industrial lipases. These topics are investigated by combining biochemical, computational, structural and biophysical approaches with rational mutagenesis.
Research interest
COLD-ACTIVE ENZYMES
Cold-active enzymes are produced by psychrophilic organisms to survive in low-temperature environments. These enzymes have developed different structural strategies to show high activity at low temperatures.
- Discovery of enzymes from psychrophilic microorganisms
- Uncovering cold adaptation mechanisms
- Biotechnological exploitation
USE OF CHEESE WHEY PERMEATE IN THE PRODUCTION OF RECOMBINANT PROTEINS
Cheese whey permeate is a by-product of the production of the valuable whey proteins obtained by ultrafiltration of cheese whey, a major by-product of the dairy industry. To valorize this waste biomass, we studied the effects of cheese whey permeate, obtained from an Italian factory, on producing recombinant proteins in Escherichia coli cells.
ICE BINDING PROTEINS
Ice-binding proteins (IBPs) are produced by organisms exposed to sub-zero temperatures to counteract the damaging effects of freezing.
- Discovery of new ice-binding proteins
- Investigation of structural elements involved in ice-binding
EFFECTS OF ORGANIC SOLVENTS ON INDUSTRIAL LIPASES
Biocatalysis in anhydrous environments provides the opportunity to extend the use of enzymes. However, in the presence of organic solvents, enzymes may undergo reversible inhibition, inactivation, or aggregation.
- Investigation of the effects of alcohol on the activity and stability of free or immobilized lipases
- Determination of structural elements involved in tolerance to organic solvents.
Research projects
“From local dairy waste to SUgar blocks for the synthesis of bioPoLymerS (SUrPLaS)”. Fondazione CARIPLO, Bando: Economia circolare per un futuro sostenibile (Grant numero: 2020-0838).
Selected articles
1. de Divitiis, M., Ami, D., Pessina, A., Palmioli, A., Sciandrone, B., Airoldi, C., Regonesi, M., R., Brambilla, L., Lotti, M., Natalello, A., Brocca, S., & Mangiagalli, M.* (2023). Cheese-whey permeate improves the fitness of Escherichia coli cells during recombinant protein production. Biotechnology for Biofuels and Bioproducts, 16(1), 1-19. doi: 10.1186/s13068-023-02281-8
2. Mangiagalli, M., Lapi, M., Maione, S., Orlando, M., Brocca, S., Pesce, A., Barbiroli, A., Camilloni, C., Lotti, M. & Nardini, M. (2021). The co‐existence of cold activity and thermal stability in an Antarctic GH42 β‐galactosidase relies on its hexametric quaternary arrangement. The FEBS Journal, 288(2), 546-565. PMID: 32363751 DOI: 10.1111/febs.15354
3. Mangiagalli, M., Ami, D., de Divitiis, M., Brocca, S., Catelani, T., Natalello, A. & Lotti, M. (2022) Short-chain alcohols inactivate an immobilized industrial lipase through two different mechanisms. Biotechnology Journal, 2100712. doi: 10.1002/biot.202100712.
4. Mangiagalli, M., Sarusi, G., Kaleda, A., Dolev, M. B., Nardone, V., Vena, V. F., ... and Nardini, M. (2018). Structure of a bacterial ice binding protein with two faces of interaction with ice. The FEBS journal, 285(9), 1653-1666. PMID: 29533528 DOI: 10.1111/febs.14434
International and national collaborations
Prof. Marco Nardini (Università di Milano)
Prof. Alberto Barbiroli (Università di Milano)
Prof. Juergen Pleiss (Stuttgart University)
Prof. Ido Braslavsky (Hebrew University of Jerusalem)
Mangiagalli’s Lab – #MangiagalliLab_BtBs
last update: August 2024