Marina Lotti graduated in Biological Sciences in Milano and got her PhD in Sciences (Naturwissenschaften) at the Max-Planck-Institut fuer Molekulare Genetik in Berlin (Germany) with a thesis of the structure of ribosomes. Presently she is a full Professor of Biochemistry at the University of Milano-Bicocca, where she leads the Laboratory of Protein Engineering and Industrial Enzymology. Currently she serves as the Head of the Department of Biotechnology and Biosciences and is a member of the Academic Senate and of the Board for the Quality of Research (PQA) of the University.
Major research topics concern enzymes employed in biocatalysis, and proteins isolated from psychrophilic organisms, in particular enzymes active at low-temperature and ice binding proteins. Another relevant issue is protein folding and misfolding, related to the aggregation of recombinant proteins to form inclusion bodies. These studies employ a combined approach of mutagenesis (both directed evolution and site directed mutagenesis) and biochemical and biophysical characterization.
Research activity is performed in collaboration with several other groups of the Department and with national and international teams.
Teaching is in the frame of the Bachelor and Master degrees in Biotechnology (Biochemistry and Industrial Biochemistry) and of the PhD program in Converging technologies for biomolecular systems. She is one of the directors of the European Summer School of Industrial Biotechnology (http://www.essib.eu/) and one of the organizers of the UNIMIB Summer School “Towards a Bio-based economy: science, innovation, economics, education”. Moreover, ML is involved in the programs of interaction with schools, that are a major goal of the Department.
Function and structure of Antarctic glycosydases
We study the features of enzymes from psychrophilic bacteria and lower eukaryotes, identified from genomic and metagenomic analysis. We studied previously superoxide dismutases and are currently engaged in the characterization and exploitation of several glycosydases. These enzymes show very diverse properties and provide hints about their evolution. From the application point of view, enzymes that perform well in the cold are of interest in any energy saving process and in the food industry.
Ice binding proteins
Ice binding proteins, previously known as antifreeze proteins, are produced by organisms exposed to temperature close or even below the freezing point of water as a protection toward the formation of intracellular ice crystals. IBP find application in cryopreservation and in the development of anti-icing materials.
We are active in the design and optimization of biocatalytic processes, even in collaboration with companies. Our favorite enzymes are lipases that we use for several purposes. A key issue for our laboratory is the mechanism of the inhibitory effect of methanol on lipase activity in the reaction of transesterification used for the biotechnological production of biodiesel. This project is a collaboration with Prof. Brocca.
In several cases, recombinant proteins aggregate to form inclusion bodies (IBs). The structure of proteins embedded in IBs can be modulated by the production conditions and, whenever a relevant amount of native structure is maintained, activity can be preserved. We have studied the mechanism of aggregation, the structure of aggregated proteins and the effects of aggregation on producing cells.
Kaleda A, Haleva L, Sarusi G, Pinsky T, Mangiagalli M, Bar-Dolev M, Lotti M, Nardini M, Braslavsky I (2019) Saturn-shaped ice burst pattern and fast basal binding of an ice-binding protein from an Antarctic bacterial consortium. Langmuir 35(23):7337-7346
Pischedda A, Priyan K, Mangiagalli M, Chiappori F, Milanesi L, Miceli C, Pucciarelli S, Lotti M (2018) Antarctic marine ciliates under stress: superoxide dismutases from the psychrophilic Euplotes focardii are cold-active yet heat tolerant enzymes. Scientific Reports (2018) 8:14721 | DOI:10.1038/s41598-018-33127-1
Mangiagalli M, Sarusi G, Kaleda A, Bar Dolev M, Nardone V, Vena VF, Braslavsky I, Lotti M*, Nardini M* (2018) Structure of a bacterial Ice Binding Protein with two faces of interaction with ice. FEBS Journal doi: 10.1111/febs.14434
Lotti M, Pleiss J, Valero F, Ferrer P. (2018) Enzymatic production of biodiesel: strategies to overcome methanol inactivation. Biotechnology J doi: 10.1002/biot.201700155