Patrizia Spizzo

TL;DR: In any study dealing with enzyme immobilisation the prerequisite is the rigorous planning and reporting of experiments, being aware of the complexity of these multi-phase systems.

TL;DR: A computational analysis of the structures of lipase B from Candida antarctica and two penicillin G acylases and PGA, from eukaryotic and prokaryotic sources, respectively, suggests the involvement of the glycan moiety in enzyme-polymer interactions.

TL;DR: Preliminary experimental data here reported indicate that covalent immobilization of lipase from Pseudomonas cepacia performed in the presence of hydrophobic solvent allows one to achieve a more than 10-fold increase in immobilization yield as compared to similar protocols performed in simple aqueous buffer.

TL;DR: The computational analysis of the three‐dimensional models proved to be an effective tool for acquiring information and allowed to formulate an optimal immobilized biocatalyst even more active that the native one, thus enabling the full exploitation of the catalytic potential of these enzymes.

TL;DR: In this paper, the use of lyophilized mycelia facilitates the separation process so that in one step the two enantiomers of flurbiprofen, which are both valuable for pharmaceutical applications, can be easily separated.