(65z) Encapsulation of Hewl Crystals IN Polymeric Networks

Protein encapsulation and crystallization are under much investigation due to the advantages they possess, such as the amount of applications that can result like the use in biosensors, drug delivery purposes, filter membrane creation, etc. Crystallization and encapsulation can also permit us to learn more about the structure and properties of the proteins. There are many advantages but the more important ones are the comfort and stability these methods offer proteins, which is very important since proteins are extremely sensitive when outside of their natural environments and the ability of manipulate the protein crystals. However, there are many other things that must be taken in consideration like pH, temperature, solvents, release, ect. All the experiments where produced using the protein lysozyme from hen egg white (HEWL), this due to the property of been more resistant to harsh conditions than other proteins. We are using two methods for protein crystallization: Batch method and the Hanging Drop method. Varying the concentrations of Methacrylic acid (anionic, MAA) and poly(ethylene glycol) dimethacrylate n=1000 (cross-linker, PEGDMA1000), adding the protein crystals to the solution and using UV Polymerization the membranes are obtained with the crystals inside the polymeric networks. The qualitative studied morphologies were: 88% MAA ? 40%Solvent, 88% MAA ? 50%Solvent, 88% MAA ? 60%Solvent, 90% MAA ? 40%Solvent, 92% MAA ? 40%Solvent, 95% MAA ? 40%Solvent, 98% MAA ? 40%Solvent and 99% MAA ? 40%Solvent. The best result were obtained at 88% MAA ? 40%Solvent (ethanol 30%), where the crystals lasts months without suffering any damage, in other words remaining intact and active or stable and their structure remain almost intact compare with the others concentration, where at time cero the crystalline structure looks very damage.