BACKGROUND Immobilization of biologically active proteins on nanosized surfaces is a key process in bionanofabrication. Carbon nanotubes with their high surface areas, as well as useful electronic, thermal and mechanical properties, constitute important building blocks in the fabrication of novel functional materials. RESULTS Lipases from Candida rugosa (CRL) were found to be adsorbed on the ...

Immobilization has emerged since last decade as a very powerful tool to improve almost all enzyme properties like stability, activity, specificity and selectivity, and reduction of inhibition. The immobilization may help to solve some of the problems of enzymes as industrial biocatalysts like enzyme recovery for reuse. In the present investigation A.niger was isolated from soil and identified b...

Analysis of immobilized enzyme in situ is a crucial step to embed an enzyme onto the planar technology of standard integrated circuit (IC) and microelectromechanical systems (MEMS) for a bioreactor or enzyme-coupled biosensor. A surface reaction limited model, based on a systematized and standardized approach, mathematically derived from mass transfer dynamics and the Michaelis-Menten equation ...

The present paper addresses two crucial features in the industrial development of fructose production by enzymatic hydrolysis of inulin: the use of immobilized biocatalyst in the hydrolysis of crude extracts of chicory roots and the evaluation of the effect of degree of polymerization of inulin on the overall reaction rate. The immobilized biocatalyst consisted of inulinase covalently bound to ...

Studies were conducted on the Bacillus sp. neutral protease immobilization on different matrices. The immobilized protease was prepared by three methods, such as entrapment on calcium alginate and gelatin; physical adsorption by celite and alumina; ionic binding by amberlite IR-120 and DEAE-cellulose. The maximum immobilization yield was obtained with celite adsorbed protease. The immobilized e...

A bacterial enzyme(s) capable of hydrolyzing nine organophosphate insecticides was covalently bound to glass. The efficiency of this binding reaction ranged from 4 to 17%. Under continuous column operation, the immobilized enzyme(s) had an extrapolated half-life of 280 days. The specific activity of this glass-covalently bound hydrolase activity for parathion varied from 0.035 to 0.15 mumol/min...

Aspergillus niger lipase immobilization by covalent binding on chitosan-coated magnetic nanoparticles (CMNP), obtained by one-step co-precipitation, was studied. Hydroxyl and amino groups of support were activated using glycidol and glutaraldehyde, respectively. Fourier transform infrared spectrometry, high-resolution transmission electron microscopy and thermogravimetric analysis confirmed rea...

S-adenosylmethionine (SAM), an important metabolite in all living organisms, has been widely used to treat various diseases. To develop a simple and efficient method to produce SAM, an engineered variant of the methionine adenosyltransferase (MAT) from Escherichia coli was investigated for its potential use in the enzymatic synthesis of SAM due to its significantly decreased product inhibition....

Several clinical laboratory methods using enzymes as reagents now may utilize immobilized enzymes. These are enzymes attached to solid surfaces by adsorption, covalent binding, cross linking or similar means. Immobilized enzymes are widely used presently in convenient tests for urine glucose and galactose or blood glucose and urea, and in serum glucose or urea determinations by automated method...

Alkaline protease from Bacillus licheniformis ATCC21415 was partially purified by fractional precipitation at 70% ethanol which showed 6.2-fold purification. Immobilization of the enzyme by physical adsorption on loofa (as a new carrier) had the highest immobilization yield (70.5%).Chemical modification of the enzyme by covalent coupling with sodium -periodate activated amylopectin retained (78...