Improvement in biochemical characteristics of cross-linked enzyme aggregates (CLEAs) with magnetic nanoparticles as support matrix.

Recent developments in novel carriers for enzyme immobilization have led to improvement in the stability and cost-effectiveness of the biocatalysts for their enhanced suitability in the industrial applications. Cross-linked enzyme aggregates (CLEAs), a recent technique developed in the carrier-free type of enzyme immobilization is a simple and straightforward method. Moreover, the magnetic property and the higher surface-to-volume ratio of the maghemite nanoparticles have also been utilized in the present immobilization technique as magnetic nanoparticle-supported CLEAs (Mgnp-CLEAs).

Understanding domain movements and interactions of Pseudomonas aeruginosa lipase with lipid molecule tristearoyl glycerol: A molecular dynamics approach.

Lipases are biocatalysts which exhibit optimal activity at the aqueous-lipid interface. Molecular Dynamics (MD) Simulation studies on lipases have revealed the structural changes occurring in the enzyme, at the loop-helix-loop, often designated as the "lid", which is responsible for its interfacial activation. In recent years, MD simulation of lipases at molecular level have been studied in detail, whereas very few studies are carried over on its interaction with lipid molecules.

Quantitative study on the effect of calcium and magnesium palmitate on the formation of Pseudomonas aeruginosa biofilm.

Calcium palmitate and magnesium palmitate (which are major constituents of waste water) are insoluble precipitates that accumulate in bodies of water. This leads to the formation of biofilms because bacterial cells can use these fatty acid salts as a carbon source. It is important to study the formation of biofilms because they cause corrosion of pipelines and water contamination.

A multisubstrate assay for lipases/esterases: assessing acyl chain length selectivity by reverse-phase high-performance liquid chromatography.

Lipases and esterases are hydrolytic enzymes and are known to hydrolyze esters with unique substrate specificity and acyl chain length selectivity. We have developed a simple competitive multiple substrate assay for determination of acyl chain length selectivity of lipases/esterases using RP-HPLC with UV detection. A method for separation and quantification of 4-nitrophenyl fatty acid esters (C4-C18) was developed and validated.