Immobilization of Candida rugosa lipase on glass beads for enantioselective hydrolysis of racemic naproxen methyl ester.

Candida rugosa lipase (CRL) was immobilized on glutaraldehyde-activated aminopropyl glass beads by using covalent binding method or sol-gel encapsulation procedure and improved considerably by fluoride-catalyzed hydrolysis of mixtures of RSi(OCH3)3 and Si(OCH3)4. The catalytic properties of the immobilized lipases were evaluated into model reactions, i.e.

Surface modification of glass beads with glutaraldehyde: characterization and their adsorption property for metal ions.

In this study, a new material that adsorbs the metal ions was prepared by modification of the glass beads surfaces with glutaraldehyde. First, the glass beads were etched with 4M NaOH solution. Then, they were reacted with 3-aminopropyl-triethoxysilane (APTES).

Immobilization of albumin on aminosilane modified superparamagnetic magnetite nanoparticles and its characterization.

Magnetite nanoparticles (NPs) were synthesized by co-precipitating Fe(2+) and Fe(3+) in an ammonia solution. Magnetite NPs coated with 3-aminopropyltriethoxysilane (APTES) were prepared by silanization reaction. After activated with glutaraldehyde (GA), human serum albumin was covalently immobilized on these magnetic NPs.