Untitled

Covalent immobilization of trypsin onto poly(2-hydroxyethyl methacrylate)/ polystyrene composite microspheres, produced by emulsifier-free seeded emulsion polymerization technique, was carried out using the cyanogen bromide method under various conditions. The highest enzymatic activities of the trypsin immobilized in this study against N-u-benzoyl-L-arginine ethyl ester and N-ce-benzoyl-L-arginine-p-nitroanilide, as low-molecular substrates and casein as a high-molecular substrate, were high, as corresponding to 80 %, 85 % and 50 % of those of free trypsin, respectively.

Section: Cnbr Activation Processsupporting

confidence: 67%

Section: Immobilization Processmentioning

confidence: 99%

Covalent immobilization of trypsin onto poly(2-hydroxyethyl methacrylate)/polystyrene composite microspheres by cyanogen bromide method and its enzymatic activity

Okubo

Kamei

Tosaki

et al. 1987

“…To determine the optimum surface properties for such applications, we have studied the adsorption behavior of bovine pancreas trypsin [8][9][10] and of rabbit anti-bovine serum albumin antibody [11][12][13] onto various polymer microspheres and their bioactivities. The studies showed that polymer microspheres pro-*) Part CVI]I of the series "Studies on Suspension and Emulsion".…”

Section: Introductionmentioning

confidence: 99%

XPS analysis (ESCA) of the surface composition of poly(styrene/2-hydroxyethyl methacrylate) microspheres produced by emulsifier-free emulsion polymerization

Okubo¹,

Yamamoto²,

Kamei³

1989

Polymer microspheres composed of various compositions of styrene and 2hydroxyethyl methacrylate (HEMA) were produced by batch emulsifier-free emulsion polymerization. The HEMA content at the surface, [I-IEMA] s , of the microspheres powdered by freeze-drying was determined by both quantitative Cl,/Ois analysis and Cls peak shape analysis of the x-ray photoelectron spectroscopic spectra. When the HEMA content in the microsphere, [HEMA]p, was less than about 5 mole 0/0, the [HEMA]s values determined by the two different methods showed good agreement. At [HEMA]p above 5 mole %, [HEMA] ~ values determined by the first method were about 15 mole % greater than those determined by the second. They both showed a similar tendency with the [HEMA], being higher than the [HEMA]p, e.g., when [HEMA]p was 1 mole0/0, [HEMA], was 11 mole %. The intensity of the satellite peak due to the z ~ ~* transition of the benzene ring of the styrene component decreased with an increase in [HEMA]p, to zero at 5 mole 0/0 of [HEMA]p. These results indicate that the HEMA component is localized at the surface.

“…We have been trying to immobilize enzymes and antibody molecules onto the submicron-size monodisperse polymer microspheres produced by emulsifier-free emulsion polymerization [3,4]. Our results have shown that the surface properties, especially the surface hydrophilicities and heterogeneities, greatly affect the amount of immobilization and those bioactivities [5][6][7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

Preferential adsorption of bovine serum albumin dimer onto polymer microspheres having a heterogeneous surface consisting of hydrophobic and hydrophilic parts

Okubo

Azume

Yamamoto

1990

The adsorption behaviors of bovine serum albumin (BSA) containing both dimeric and monomeric species onto polymer microspheres were examined using various h0mopolymers and poly(2-hydroxyethyl methacrylate)/polystyrene composite microspheres which were produced by the emulsifier-free (seeded) emulsion polymerization technique. The preferential adsorption of the BSA dimer was clearly observed in an optimum region of the surface hydrophilicities of the polymer microspheres. The preferential adsorption of the BSA dimer onto the composite polymer microspheres having heterogeneous surfaces consisting of hydrophiIic and hydrophobic parts was more marked than those onto the homopolymer and copolymer microspheres having homogeneous surfaces.