RESUMO
The development of robust biocatalysts with increased stability and activity is a major challenge to industry. A major breakthrough in this field was the development of cross-linked enzyme crystals with high specificity and stability. A method is described to produce micro crystals of CLEC lipase, which is thermostable and solvent stable. Lipase from Burkholderia cepacia was crystallized using ammonium sulfate and cross-linked with glutaraldehyde to produce catalytically active enzyme. The maximum yield of CLEC was obtained with 70% ammonium sulfate and cross-linked with 5% (v/v) glutaraldehyde. SEM studies showed small hexagonal-shaped crystals of 2-5 microm size. CLEC lipase had improved thermal and reuse stability. It is versatile, having good activity in both polar and nonpolar organic solvents. CLEC lipase was coated using beta cyclodextrin for improving the storage and reuse stability. CLEC was successfully used for esterification of Ibuprofen and synthesis of ethyl butyrate.
Assuntos
Reagentes de Ligações Cruzadas/química , Cristalização/métodos , Lipase/química , Lipase/ultraestrutura , Catálise , Ativação Enzimática , Estabilidade Enzimática , Tamanho da Partícula , Conformação ProteicaRESUMO
The synthesis of modified hydrophobic starch nanoparticles using long chain fatty acids was accomplished. Grafting of fatty acid on the starch was done using potassium persulphate as catalyst and the formation of graft polymer was confirmed by FTIR spectra. The thermal properties of the native and grafted starch were investigated using simultaneous TG-DTA and DSC. The graft polymerization was found to be depending on the temperature and the duration of the reaction. The modified starch nanoparticles were cross-linked with sodium tripoly phosphate for better stabilization. Morphology of the grafted starch nanoparticles was studied by SEM and AFM. Drug-loading and the controlled release of the drug from the nanoparticles was studied using indomethacin as model drug.