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Strategic single point mutation yields a solvent- and salt-stable transaminase from Virgibacillus sp. in soluble form (2018)
Journal Article
Guidi, B., Planchestainer, M., Contente, M. L., Laurenzi, T., Eberini, I., Gourlay, L. J., …Molinari, F. (2018). Strategic single point mutation yields a solvent- and salt-stable transaminase from Virgibacillus sp. in soluble form. Scientific Reports, 8(1), doi:10.1038/s41598-018-34434-3

A new transaminase (VbTA) was identified from the genome of the halotolerant marine bacterium Virgibacillus 21D and its expression resulted in the production of an insoluble protein in E. coli. After a single mutation identified through sequence homo... Read More

Biocatalytic N-acylation of amines in water using an acyltransferase from Mycobacterium smegmatis (2018)
Journal Article
Contente, M., Pinto, A., Molinari, F., & Paradisi, F. (2018). Biocatalytic N-acylation of amines in water using an acyltransferase from Mycobacterium smegmatis. Advanced Synthesis and Catalysis, doi:10.1002/adsc.201801061. ISSN 1615-4150

A straightforward one-step biocatalyzed synthesis of different N-acyl amides in water was accomplished using the versatile and chemoselective acyltransferase from Mycobacterium smegmatis (MsAcT). Acetylation of primary arylalkyl amines was achieved w... Read More

Self-sustaining closed-loop multienzyme mediated conversion of amines into alcohols in continuous reactions (2018)
Journal Article
Contente, M. L., & Paradisi, F. (2018). Self-sustaining closed-loop multienzyme mediated conversion of amines into alcohols in continuous reactions. Nature Catalysis, 1, 452–459. doi:10.1038/s41929-018-0082-9

The synthesis of alcohols from amines starting material is an excellent, yet challenging, strategy for the preparation of pharmaceuticals and polymers. Here, we developed a versatile, self-sustaining closed-loop multienzymatic platform for the biocat... Read More

Genetically fused T4L acts as a shield in covalent enzyme immobilisation enhancing the rescued activity (2018)
Journal Article
Planchestainer, M., Padrosa, D. R., Contente, M. L., & Paradisi, F. (2018). Genetically fused T4L acts as a shield in covalent enzyme immobilisation enhancing the rescued activity. Catalysts, 8(1), doi:10.3390/catal8010040. ISSN 2073-4344

Enzyme immobilisation is a common strategy to increase enzymes resistance and reusability in a variety of excellent ‘green’ applications. However, the interaction with the solid support often leads to diminished specific activity, especially when non... Read More

A stereospecific carboxyl esterase from Bacillus coagulans hosting nonlipase activity within a lipase-like fold (2018)
Journal Article
De Vitis, V., Nakhnoukh, C., Pinto, A., Contente, M. L., Barbiroli, A., Milani, M., …Romano, D. (in press). A stereospecific carboxyl esterase from Bacillus coagulans hosting nonlipase activity within a lipase-like fold. FEBS Journal, doi:10.1111/febs.14368. ISSN 1742-464X

Microbial carboxylesterases are important biocatalysts that selectively hydrolyze an extensive range of esters. Here, we report the biochemical and structural characterization of an atypical carboxylesterase from Bacillus coagulans (BCE), endowed wit... Read More

Highly efficient oxidation of amines to aldehydes via flow-based biocatalysis (2017)
Journal Article
Contente, M. L., Dall'Oglio, F., Tamborini, L., Molinari, F., & Paradisi, F. (in press). Highly efficient oxidation of amines to aldehydes via flow-based biocatalysis. ChemCatChem, doi:10.1002/cctc.201701147. ISSN 1867-3880

A new mild and efficient process for the preparation of aldehydes in water employed as flavour and fragrance components in food, beverage, cosmetics, as well as in pharmaceuticals was developed using a continuous-flow approach based on an immobilized... Read More

Stereoelectronic effects in the reaction of aromatic substrates catalysed by Halomonas elongata transaminase and its mutants (2016)
Journal Article
Contente, M. L., Planchestainer, M., Molinari, F., & Paradisi, F. (in press). Stereoelectronic effects in the reaction of aromatic substrates catalysed by Halomonas elongata transaminase and its mutants. Organic and Biomolecular Chemistry, 14, doi:10.1039/C6OB01629D. ISSN 1477-0520

A transaminase from Halomonas elongata and four mutants generated by an in silico-based design, were recombinantly produced in E. coli, purified and applied to the amination of mono-substituted aromatic carbonyl-derivatives. While benzaldehyde deriva... Read More