Lysozyme-Responsive Hydrogels of Chitosan-Streptomycin Conjugates for the On-Demand Release of Biofilm-Dispersing Enzymes for the Efficient Eradication of Oral Biofilms.

Hydrogels with controlled degradation and sustained antibiofilm activity are promising biomaterials for the treatment of oral infections such as periodontitis or caries. In this article, an forming chitosan-streptomycin hydrogel is developed that can target established bacterial biofilms in response to lysozyme, an enzyme that is overexpressed in saliva during oral infections. When the new hydrogel is applied to simulated oral biofilms, the overexpressed lysozyme degrades the hydrogel and releases chitosan-streptomycin oligosaccharides that can eradicate the biofilm.

Chitosan sulfate-lysozyme hybrid hydrogels as platforms with fine-tuned degradability and sustained inherent antibiotic and antioxidant activities.

The control of the properties and biological activities of chitosan-lysozyme hybrid hydrogels to exploit their interesting biomedical applications depends largely on the chitosan acetylation pattern, a difficult parameter to control. Herein, we have prepared sulfated chitosan-lysozyme hydrogels as versatile platforms with fine-tuned degradability and persistent bactericidal and antioxidant properties. The use of chitosan sulfates instead of chitosan has the advantage that the rate and mechanisms of lysozyme release, as well as antibacterial and antioxidant activities, depend on the sulfation profile, a structural parameter that is easily controlled by simple chemical modifications.

Thermostability Engineering of a Class II Pyruvate Aldolase from by Folding Interference.

The use of enzymes in industrial processes is often limited by the unavailability of biocatalysts with prolonged stability. Thermostable enzymes allow increased process temperature and thus higher substrate and product solubility, reuse of expensive biocatalysts, resistance against organic solvents, and better "evolvability" of enzymes. In this work, we have used an activity-independent method for the selection of thermostable variants of any protein in through folding interference at high temperature of a thermostable antibiotic reporter protein at the C-terminus of a fusion protein.

Hypoxanthine-Guanine Phosphoribosyltransferase/adenylate Kinase From : A Bifunctional Catalyst for the Synthesis of Nucleoside-5'-Mono-, Di- and Triphosphates.

In our search for novel biocatalysts for the synthesis of nucleic acid derivatives, we found a good candidate in a putative dual-domain hypoxanthine-guanine phosphoribosyltransferase (HGPRT)/adenylate kinase (AMPK) from (HGPRT/AMPK). In this respect, we report for the first time the recombinant expression, production, and characterization of a bifunctional HGPRT/AMPK. Biochemical characterization of the recombinant protein indicates that the enzyme is a homodimer, with high activity in the pH range 6-7 and in a temperature interval from 30 to 80°C.