Marina Lotti

ORCID: 0000-0001-5419-7572
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About
Contact & Profiles
Research Areas
  • Enzyme Catalysis and Immobilization
  • Microbial Metabolic Engineering and Bioproduction
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Bacterial Genetics and Biotechnology
  • Enzyme Production and Characterization
  • Biofuel production and bioconversion
  • Protein purification and stability
  • RNA and protein synthesis mechanisms
  • Analytical Chemistry and Chromatography
  • Fungal and yeast genetics research
  • Physiological and biochemical adaptations
  • Carbohydrate Chemistry and Synthesis
  • Monoclonal and Polyclonal Antibodies Research
  • Antifungal resistance and susceptibility
  • Peptidase Inhibition and Analysis
  • Electrochemical sensors and biosensors
  • Bacteriophages and microbial interactions
  • Enzyme-mediated dye degradation
  • Mass Spectrometry Techniques and Applications
  • Glycosylation and Glycoproteins Research
  • Viral Infectious Diseases and Gene Expression in Insects
  • Microbial Community Ecology and Physiology
  • Pancreatic function and diabetes
  • Protein Interaction Studies and Fluorescence Analysis

University of Milano-Bicocca
2016-2025

University of Bologna
2023

Hebrew University of Jerusalem
2016

University of Milan
1997-2011

University of Bari Aldo Moro
1995

Max Planck Society
1983-1989

Max Planck Institute for Molecular Genetics
1984-1985

Yeast strains endowed with robustness towards copper and/or enriched in intracellular Cu might find application biotechnology processes, among others the production of functional foods. Moreover, they can contribute to study human diseases related impairments metabolism. In this study, we investigated molecular and physiological factors that confer tolerance baker's yeasts.We characterized effects elicited natural Candida humilis Saccharomyces cerevisiae by exposure culture broth. We...

10.1186/1475-2859-11-1 article EN cc-by Microbial Cell Factories 2012-01-03

Oxidative stress is a particularly severe threat to Antarctic marine polar organisms because they are exposed high dissolved oxygen and intense UV radiation. This paper reports the features of three superoxide dismutases from psychrophilic ciliate Euplotes focardii that faces two environmental challenges, oxidative low temperature. Two out these Cu,Zn (named Ef-SOD1a Ef-SOD1b) one belongs Mn-containing group (Ef-SOD2). Ef-SOD1s Ef-SOD2 differ in their evolutionary history, expression overall...

10.1038/s41598-018-33127-1 article EN cc-by Scientific Reports 2018-09-27

The secondary structure of lipase 1 from Candida rugosa, a model system for large monomeric enzymes, has been studied by FTIR (Fourier-transform infrared) spectroscopy in water and 2H2O. content, determined the analysis amide I band absorption through second derivative curve fitting procedures, is agreement with that estimated X-ray data predicts, addition, existence two classes α-helices. We have also investigated enzyme stability aggregation at high temperature following protein unfolding....

10.1042/bj20041296 article EN Biochemical Journal 2005-01-07

The production of synthetic plastics, especially polyethylene, has reached a crucial level, making highly challenging plastic waste management. This paper aims to elucidate the role two novel laccase-like multicopper oxidases in polyethylene oxidative degradation based on transcriptomic data from Rhodococcus opacus R7 grown polyethylene. purification recombinant proteins, LMCO2 and LMCO3 belonging respectively three- two-domains laccase families, showed that they are endowed with different...

10.1016/j.eti.2023.103273 article EN cc-by-nc-nd Environmental Technology & Innovation 2023-07-07

Abstract The fungus Candida rugosa produces multiple lipase isoenzymes (CRLs) with distinct differences in substrate specificity, particular regard to selectivity toward the fatty acyl chain length. Moreover, isoform CRL3 displays high activity towards cholesterol esters. Lipase share over 80% sequence identity but diverge of lid, a mobile loop that modulates access active site. In enzyme conformation, open lid participates substrate‐binding site and contributes recognition. To address role...

10.1110/ps.0304003 article EN Protein Science 2003-09-19

Cold environments are populated by organisms able to contravene deleterious effects of low temperature diverse adaptive strategies, including the production ice binding proteins (IBPs) that inhibit growth crystals inside and outside cells. We describe properties such a protein (EfcIBP) identified in metagenome an Antarctic biological consortium composed ciliate Euplotes focardii psychrophilic non-cultured bacteria. Recombinant EfcIBP can resist freezing without any conformational damage is...

10.1111/febs.13965 article EN FEBS Journal 2016-11-17

A recombinant lipase cloned from Pseudomonas fragi strain IFO 3458 (PFL) was found to retain significant activity at low temperature. In an attempt elucidate the structural basis of this behaviour, a model its three‐dimensional structure built by homology and compared with homologous mesophilic lipases, i.e. aeruginosa (45% sequence identity) Burkholderia cepacia (38%). model, features common all known lipases have been identified, such as catalytic triad (S83, D238 H260) oxyanion hole (L17,...

10.1046/j.1432-1033.2002.03012.x article EN European Journal of Biochemistry 2002-07-01

Several fungi secrete lipase isozymes differing in biochemical properties and some cases substrate specificity. In the yeast Candida rugosa, a family of related genes encodes for multiple proteins, highly homologous sequence but partially different regions interacting with molecule. Analysis these substitutions performed on basis alignments using 3-D model enzyme, allows identification restricted number amino acids possibly involved specificity lipases.

10.1093/protein/7.4.531 article EN Protein Engineering Design and Selection 1994-01-01

The cold‐adapted Pseudomonas fragi lipase (PFL) displays highest activity on short‐chain triglyceride substrates and is rapidly inactivated at moderate temperature. Sequence structure comparison with homologous lipases endowed different substrate specificity stability, pointed to three polar residues in the lid region, that were replaced amino acids conserved equivalent positions reference lipases. Substitutions T137 T138 modified chain‐length preference profile, increasing relative towards...

10.1016/j.febslet.2005.03.037 article EN FEBS Letters 2005-03-31

The aggregation of a recombinant lipase as inclusion bodies (IBs) was studied directly within intact Escherichia coli cells by FT‐IR microspectroscopy. Through this approach, it possible to monitor in real time the different kinetics IB formation at 37 and 27 °C, excellent agreement with results SDS–PAGE analysis. Furthermore, insights on residual native‐like structure expressed protein – both isolated inside were obtained secondary analysis Amide I band spectra.

10.1016/j.febslet.2005.04.085 article EN FEBS Letters 2005-05-31

In living organisms, copper (Cu) contributes to essential functions but at high concentrations it may elicit toxic effects. Cu-tolerant yeast strains are of relevance for both biotechnological applications and studying physiological molecular mechanisms involved in stress resistance. One way obtain tolerant is exploit experimental methods that rely on the principles natural evolution (evolutionary engineering) allow development complex phenotypic traits. However, most cases, basis changes...

10.1099/mic.0.058024-0 article EN Microbiology 2012-07-13

To survive in cold environments, psychrophilic organisms produce enzymes endowed with high specific activity at low temperature. The structure of these is usually flexible and mostly thermolabile. In this work, we investigate the structural basis adaptation a GH42 β-galactosidase from Marinomonas ef1. This enzyme couples astonishing robustness for protein, it retains 23% its highest 5 °C stable several days 37 even 50 °C. Phylogenetic analyses indicate close relationship thermophilic...

10.1111/febs.15354 article EN FEBS Journal 2020-05-04

Broadly used in biocatalysis as acyl acceptors or (co)-solvents, short-chain alcohols often cause irreversible loss of enzyme activity. Understanding the mechanisms inactivation is a necessary step toward optimization biocatalytic reactions and design enzyme-based sustainable processes. The functional structural responses an immobilized enzyme, Novozym 435 (N-435), exposed to methanol, ethanol, tert-butanol, are explored this work. N-435 consists Candida antarctica lipase B (CALB) adsorbed...

10.1002/biot.202100712 article EN cc-by Biotechnology Journal 2022-02-21

Laccases that oxidize low‐density polyethylene (LDPE) represent a promising strategy for bioremediation purposes. To rationalize or optimize their PE‐oxidative activity, two fundamental factors must be considered: the enzyme's redox potential and its binding affinity/mode towards LDPE. Indeed, stable laccase‐PE complex may facilitate thermodynamically unfavorable electron transfer, even without mediators. In this study, we compared LDPE‐binding properties of three different PE‐oxidizing...

10.1002/cssc.202402253 article EN ChemSusChem 2025-01-10
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