Design of an antibacterial gelatin based on a covalent protein–protein coupling

An antibacterial peptide (AMP), i.e., nisin, was covalently bound to gelatin through a protein–protein coupling. Various reaction conditions were tested to study and optimize parameters of grafting e.g., orientation and density of AMP, which could impact the final antibacterial activity of the modified biopolymer. Modification was investigated by Fourier transform infrared (FT‐IR) spectroscopy and zeta potential. The antibacterial activity of the nisin‐enriched gelatin was evaluated against two staphylococci bacterial strains, i.e., Staphylococus epidermidis and Staphylococcus aureus. A higher activity was found for gelatin modified at pH = 7.4 revealing an influence of the nisin orientation on the protein antibacterial property. © 2014 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2015 , 132, 41825.     

Trifluoroacetic Acid Hydroxylamine System as Organocatalyst Reagent in a One-Pot Salt Free Process for the Synthesis of Caprolactam and Amides of Industrial Interest

Catalysis Letters - In this work we studied the reactivity of the Trifluoroacetic acid hydroxylamine system in the one step salt free synthesis of amides from ketones. A particular regards was paid...     

Energy Recovery in Pressurized Hydraulic Networks

Water Resources Management - This paper aims to evaluate the possibility of using non-utilized hydraulic energy in urban water distribution systems. For this purpose, the viability and possible...