Electrostatic immobilization of glucose oxidase in a weak acid, polyelectrolyte hyperbranched ultrathin film on gold: fabrication, characterization, and enzymatic activity.

نویسندگان

  • J G Franchina
  • W M Lackowski
  • D L Dermody
  • R M Crooks
  • D E Bergbreiter
  • K Sirkar
  • R J Russell
  • M V Pishko
چکیده

In this paper we show that hyperbranched polymers can be used as a host matrix for electrostatic entrapment of enzymes. Specifically, amine-functionalized glucose oxidase (GOx+) and horseradish peroxidase, as well as poly(amidoamine) dendrimer-modified horseradish peroxidase, reversibly sorb into polyanionic, hyperbranched poly(sodium acrylate) (PAA-) films that are on the order of a few hundred angstroms thick. The quantity of GOx+ entrapped within the PAA- films depends on the nature of film preparation but is typically on the order of 0.06 unit/cm2. The extent to which entrapped GOx+ retains its activity depends on the film history, but for PAA-/GOx+ composites not exposed to glucose and stored at 4 degrees C, the original activity is retained for up to 68 days and perhaps longer.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Construction of layer-by-layer self-assemblies of glucose oxidase and cationic polyelectrolyte onto glassy carbon electrodes and electrochemical study of the redox-mediated enzymatic activity

Build-up of enzyme–polyelectrolyte multilayer onto glassy carbon (GC) surfaces by electrostatic self-assembling method has been investigated. In order to functionalize GC surface by a starting negatively charged layer, two approaches have been carried out: (i) covalent linkage of phenyl acetic acid through electroreduction of 4-phenylacetic diazonium salt (GCA surface), and (ii) formation of a ...

متن کامل

Layer-by-layer-assembled microfiltration membranes for biomolecule immobilization and enzymatic catalysis.

Multilayer assemblies of polyelectrolytes, for protein immobilization, have been created within the membrane pore domain. This approach was taken for two reasons: (1) the high internal membrane area can potentially increase the amount of immobilized protein, and (2) the use of convective flow allows uniform assembly of layers and eliminates diffusional limitations after immobilization. To build...

متن کامل

Characterization of oxidoreductase–redox polymer electrostatic film assembly on gold by surface plasmon resonance spectroscopy and Fourier transform infrared–external reflection spectroscopy

The electrostatic assembly of nanocomposite thin films consisting of alternating layers of an organometallic redox polymer (RP) and oxidoreductase enzymes, glucose oxidase (GOX), lactate oxidase (LOX) and pyruvate oxidase (PYX), was investigated. Multilayer nanostructures were fabricated on gold surfaces by the deposition of an anionic self-assembled monolayer of 11-mercaptoundecanoic acid, fol...

متن کامل

Design and Fabrication of Glucose/O2 Enzymatic Biofuel Cell

Enzyme-based biofuel cells (EBFCs) are systems that use a variety of organic compounds to produce electricity through oxido-reductase enzymes, such as oxidase or dehydrogenase as biocatalysts immobilized on electrodes. In this study, a single-chamber EBFC consisting of carbon electrodes that operating at ambient temperature in phosphate buffer, pH 7 is reported. The EBFC anode was based on gluc...

متن کامل

A Simple Image Analysis Method for Determination of Glucose by using Glucose Oxidase CdTe/TGA Quantum Dots

Glucose, as the major energy source in cellular metabolism, plays an important role in the natural growth of cells. Herein, a simple, rapid and low-cost method for the glucose determination by utilizing glucose oxidase and CdTe/thioglycolic acid (TGA) quantum dots (QDs) on a thin layer chromatography (TLC) plate has been described. The detection was based on the combination of the glucose enzym...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Analytical chemistry

دوره 71 15  شماره 

صفحات  -

تاریخ انتشار 1999