New publication:                                                                         

our optimized mammalian cells culture platform has been used to successfully express and purify a number of human recombinant proteins. As a paradigm, our established protocol has been efficiently adapted to rapidly produce the receptor binding domain (RBD) of SARS-CoV-2S protein in CHO cells. 

Rosini and Pollegioni, 2022. Biotechnol. Appl. Biochemhttps://doi.org/10.1002/bab.2409.                

CHO 2022.jpg

The research article by E. Vignali, et al. has been selected as front cover in ChemSusChem: this image shows the formation of low-molecular-weight compounds by the oxidative depolymerization of lignin by the laccase-Lig multienzymatic multistep system.                                                                                                       


New publications:                                                                            

cell reports 2022.jpg

Maffioli et al., 2022. Cell Reports. https://doi.org/10.1016/j.celrep.2022.111271.                                          

In this work, we report a multi-omics analysis of the hippocampus of individuals with Alzheimer’s disease and healthy controls. Our study highlights a strong sex effect under normal aging and AD conditions: we observed a decrease in insulin response in AD when comparing the female with the male group; and also a significant modulation of serine metabolism.                                                                                      

A new multienzymatic multistep system for lignin valorization was designed and developed.
Lignin depolymerization through selective and specific enzymatic treatments is a key aspect in the biotechnological valorization of this biopolymer.
Qualitative and quantitative analyses permitted a more comprehensive elucidation of the effect of each biocatalyst used towards the development of a suitable method to obtain value-added end products from technical lignins of different botanical origin.



Can you believe that plastic can be fully degraded simply by an enzyme in water and within hours? Watch for yourself!

We produced a newly engineered biocatalyst capable of breaking down more than 95% of PET in only 48 hours of incubation at 60 °C, without adding chemicals or using high temperatures. Enzyme-based PET biodegradation represents a useful tool and a feasible solution for the development of sustainable, environmental-friendly, and cost-effective processes for plastic recycling in a perspective of the circular economy.

Pirillo et al., 2022. Int. J. Mol. Sci. doi: 10.3390/ijms23010264.                                        


New publication: 


in this work, we report on a straightforward workflow employing semi-rational protein engineering combined to a high-throughput screening of variant libraries for their activity on PET nanoparticles.  The present workflow is a well-suited protocol for the evolution of PET-hydrolysing enzymes to help generate an efficient enzymatic toolbox for the biodegradation of post-consumer PET into its main molecular components.   

Pirillo et al., 2022. Int. J. Mol. Sci. doi: 10.3390/ijms23010264.                                                       


New review available on D-amino acids as novel blood-based biomarkers.

Murtas and Pollegioni, 2021. Curr Med Chem. doi: 10.2174/0929867328666211125092438.



New review available on anticancer therapy based on oxidases that produce reactive oxygen species.

Rosini and Pollegioni, 2021. Biofactors. doi: 10.1002/biof.1789.


New publication:                                                                             


Vignali et al., 2021. Advanced Synthesis & Catalysis. doi.org/10.1002/adsc.202100849.                                              

in this work, we reported the first multi-enzymatic one-pot bioconversion of vanillin into cis,cis-muconic acid (ccMA), which is widely used for the production of biodegradable plastic materials. Our proposed biocatalytic system represents a sustainable alternative for the eco-friendly production of a high value-added compound from underutilized lignin, a primary target of the bioeconomy.                                                                                          

JULY 2021

Professor Loredano Pollegioni has been elected Treasurer of the International Union of Biochemistry and Molecular Biology.

LP election IUBMB_edited_edited.jpg
LP election IUBMB_edited_edited.jpg

Antibody-drug conjugates, also named “armed antibodies”, can direct drugs to specific tissues. Here an evolved version of the ROS-generating enzyme D-amino acid oxidase was delivered to tumors by generating a chimeric protein with the F8 antibody against EDA of fibronectin, a protein abundantly expressed in the subendothelial extracellular matrix of tumor vessels. The recombinant chimeric protein produced in E. coli cells generates a strong cytotoxicity to tumor cells following the supplementation of the pro-drug D-alanine, especially when an inhibitor of the antioxidant systems is used.

Rendered with 3D Protein Imaging

APRIL 2021

New publication:

the human enzyme D-3-phosphoglycerate dehydrogenase catalyzes the first step of the L-serine biosynthesis, which plays an important role in numerous physiological functions. This enzyme is involved in cancer progression and several neurological disorders. Here is our new publication on PHGDH biochemical properties, part of the PRIN project “Dissecting serine metabolism in the brain”. https://www.mdpi.com/1422-0067/22/8/4231/htm

The cover art by Valentina Pirillo has been selected in The FEBS Journal Cover Competition 2021:   

this image is an artist representation of a plastic-degrading enzyme (PET hydrolase) that is correlated with the recent Emerging Methods and Technologies article published in The FEBS Journal: ‘Analytical methods for the investigation of enzyme-catalyzed degradation of polyethylene terephthalate’ by Valentina Pirillo, Loredano Pollegioni and Gianluca Molla.                                                                                                                                




Elena Rosini produced the recombinant SARS-CoV-2 Spike (S) protein. The coronavirus spike protein plays a key role in the early steps of COVID-19 viral infection, mainly through the interaction with the human angiotensin-converting enzyme 2 (ACE2) present on the surface of alveolar epithelial cells. Both the full-length and a truncated form (containing only the receptor binding domain) of S-protein are available at "The Protein Factory 2.0" lab and can be used to develop new diagnostic tools.

foto spike.jpeg