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Preparation of high-capacity supports containing protein G immobilized to porous silica.

ABSTRACT: This study examined the preparation of high-capacity silica supports containing immobilized protein G. A maximum content of 39 mg protein G/g silica was obtained when using 100 A pore size silica, followed by 33 mg/g for 50 A silica and 9.3-24 mg/g for 300-4000 A silica. The surface coverage of protein G increased with pore size, with a maximum level of 0.037 micromol/m(2) being obtained for 4000 A silica. These supports gave comparable apparent activities (i.e., 30-47% binding to rabbit immunoglobulin G [IgG]), with the highest binding capacities (71-77 mg IgG/g silica) being obtained for 50-100 A silica.

SUBMITTER: Jackson AJ

PROVIDER: S-EPMC2935639 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

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Preparation of high-capacity supports containing protein G immobilized to porous silica.

Jackson Abby J AJ Karle Elizabeth M EM Hage David S DS

Analytical biochemistry 20100803 2

This study examined the preparation of high-capacity silica supports containing immobilized protein G. A maximum content of 39 mg protein G/g silica was obtained when using 100 A pore size silica, followed by 33 mg/g for 50 A silica and 9.3-24 mg/g for 300-4000 A silica. The surface coverage of protein G increased with pore size, with a maximum level of 0.037 micromol/m(2) being obtained for 4000 A silica. These supports gave comparable apparent activities (i.e., 30-47% binding to rabbit immunog ...[more]

PMID: 20624371

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Project description:In this study, we immobilized pectinase preparation on porous zeolite ZSM-5 as an enzyme carrier. We realized this immobilized enzyme catalyst, pectinase preparation@ZSM-5, via a simple combined strategy involving the van der Waals adsorption of pectinase preparation followed by crosslinking of the adsorbed pectinase preparation with glutaraldehyde over ZSM-5. Conformal pectinase preparation coverage of various ZSM-5 supports was achieved for the as-prepared pectinase preparation@ZSM-5. The porous pectinase preparation@ZSM-5 catalyst exhibited ultra-efficient biocatalytic activity for hydrolyzing the β-glycosidic bonds in the model substrate 4-nitrophenyl β-D-glucopyranoside, with a broad operating temperature range, high thermal stability, and excellent reusability. The relative activity of pectinase preparation@ZSM-5 at a high temperature (70 °C) was nine times higher than that of free pectinase preparation. Using thermal inactivation kinetic analysis based on the Arrhenius law, pectinase preparation@ZSM-5 showed higher activation energy for denaturation (315 kJ mol-1) and a longer half-life (62 min-1) than free pectinase preparation. Moreover, a Michaelis-Menten enzyme kinetic analysis indicated a higher maximal reaction velocity for pectinase preparation@ZSM-5 (0.22 µmol mg-1 min-1). This enhanced reactivity was attributed to the microstructure of the immobilized pectinase preparation@ZSM-5, which offered a heterogeneous reaction system that decreased the substrate-pectinase preparation binding affinity and modulated the kinetic characteristics of the enzyme. Additionally, pectinase preparation@ZSM-5 showed the best ethanol tolerance among all the reported pectinase preparation-immobilized catalysts, and an activity 247% higher than that of free pectinase preparation at a 10% (v/v) ethanol concentration was measured. Furthermore, pectinase preparation@ZSM-5 exhibited potential for practical engineering applications, promoting the hydrolysis of β-glycosidic bonds in baicalin to convert it into baicalein. This was achieved with a 98% conversion rate, i.e., 320% higher than that of the free enzyme.

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Preparation of high-capacity supports containing protein G immobilized to porous silica.

Publications

Preparation of high-capacity supports containing protein G immobilized to porous silica.

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