A variety of nano-carriers, nano-particles, nano-fibers, nano-tubes etc. have displayed greater competence to mimic nanoscale environment for the enzyme as compared to microand macro-environments provided by traditional support carriers that have been commonly employed for enzyme immobilization. The porous structured beads (silica, alginate etc.), membranes and fibers (>100 μm) have some inhere...

Multipoint covalent immobilization of enzymes (through very short spacer arms) on support surfaces promotes a very interesting 'rigidification' of protein molecules. In this case, the relative positions of each residue of the enzyme involved in the immobilization process have to be preserved unchanged during any conformational change induced on the immobilized enzyme by any distorting agent (he...

An extracellular alkaline protease producing B. amyloliquefaciens SP1 was isolated from apple rhizosphere having multifarious plant growth-promoting activities. B. amyloliquefaciens SP1 protease was immobilized using various concentrations of calcium alginate, agar and polyacrylamide to determine the optimum concentration for formation of the beads. Enzyme activity before immobilization (at 60 ...

Enzyme immobilization has become a key strategy to improve the stability and recycling of biocatalysts, resulting in greener more cost-efficient processes. The design immobilized catalysts is often focused only on strategy, binding chemistry between enzyme support, while less attention been paid physico-chemical properties material supports. Selecting best carrier for specific application may g...

Kinetic comparisons have been made between a randomly immobilized and a site-specifically immobilized subtilisin BPN' on microfiltration membranes of varying hydrophilicities in both aqueous and organic media. Site-directed mutagenesis was employed to introduce a single cysteine into the amino acid sequence of subtilisin at a location away from the active site. Immobilization of this mutant enz...

Because the cholesterol oxidase from Brevibacterium sp. M201008 was not as stable as the free enzyme form, it had been covalently immobilized onto chemically modified Sepharose particles via N-ethyl-N'-3-dimethylaminopropyl carbodiimide. The optimum immobilization conditions were determined, and the immobilized enzyme activity obtained was 12.01 U/g Sepharose-ethylenediamine. The immobilization...

Förster resonance energy transfer (FRET) has been used to show that the average distance between proteins decreases when the protein is immobilized within polymer scaffolds, indicating that the immobilization process is inducing aggregation.