Antimicrobial geopolymer paints based on modified natural zeolite

Many antimicrobial coatings deliver a peak release of antimicrobial agent at an early age, after which they lost antimicrobial activity over time. In the present study a novel geopolymer paints with long term antimicrobial activity were developed based on natural zeolite modified with silver and copper ions. The obtained geopolymer paints were applied by brushing on concrete, ceramic, gypsum paperboard and steel. The coating was characterized by excellent adhesive strength and hiding properties. The long-term antimicrobial effect was evaluated by accelerated aging in carbonation chamber. Microstructural changes were analyzed by powder X-ray diffraction and Fourier transformed infrared spectroscopy. Cytotoxicity, antibacterial, antifungal and virucidal properties were investigated on raw and carbonated geopolymer paints. Geopolymer paints based on modified natural zeolite seems promising antimicrobial coating material that can be implemented in the global fight against the spread of diseases and pathogens

Structural and functional characterization of cold-active sialidase isolated from Antarctic fungus Penicillium griseofulvum P29

The fungal strain, Penicillium griseofulvum P29, isolated from a soil sample taken from Terra Nova Bay, Antarctica, was found to be a good producer of sialidase (P29). The present study was focused on the purification and structural characterization of the enzyme. P29 enzyme was purified using a Q-Sepharose column and fast performance liquid chromatography separation on a Mono Q column. The determined molecular mass of the purified enzyme of 40 kDa by SDS-PAGE and 39924.40 Da by matrix desorption/ionization mass spectrometry (MALDI-TOF/MS) analysis correlated well with the calculated mass (39903.75 kDa) from the amino acid sequence of the enzyme. P29 sialidase shows a temperature optimum of 37 °C and low-temperature stability, confirming its cold-active nature. The enzyme is more active towards α(2 → 3) sialyl linkages than those containing α(2 → 6) linkages.Based on the determined amino acid sequence and 3D structural modeling, a 3D model of P29 sialidase was presented, and the properties of the enzyme were explained. The conformational stability of the enzyme was followed by fluorescence spectroscopy, and the new enzyme was found to be conformationally stable in the neutral pH range of pH 6 to pH 9. In addition, the enzyme was more stable in an alkaline environment than in an acidic environment. The purified cold-active enzyme is the only sialidase produced and characterized from Antarctic fungi to date