Abstract

The separation, reusability and high catalytic activity of bioconjugate remain challenging task in proteins bound gold nanoparticles. A facile synthetic route for the fabrication of gold nanoparticle assembled polyurethane microsphere template and immobilization of trypsin on gold/polyurethane surface to form trypsin-nanogold-polyurethane bioconjugate was developed. The bioconjugate was characterized by X-ray diffraction, Field emission scanning electron microscopy, Transmission electron microscopy, UV-visible, Fourier transform infrared, Fluorescence and Circular dichroism spectroscopy. The catalytic studies confirmed retention of approximately 40% of its original activity even after eight consecutive reaction cycles. The bioconjugate is also very effective for its separation from the reaction medium and exhibited significant enhanced stability over a wide range of pH and temperature compared to free trypsin. These findings clearly demonstrate that trypsin immobilized gold nanoparticle assembled polyurethane microsphere acts as an excellent recyclable biocatalyst with enzyme-specific biocompatibility.

Authors

Kotal M, Srivastava SK, Maiti TK

Institution

Inorganic Materials and Nanocomposite Laboratory, Department of Chemistry, Indian Institute of Technology, Kharagpur 721302, India.

Source

Journal of nanoscience and nanotechnology 11:11 2011 Nov pg 10149-57

MeSH

Bioreactors
Enzyme Stability
Enzymes, Immobilized
Equipment Reuse
Gold
Hydrogen-Ion Concentration
Metal Nanoparticles
Microspheres
Nanoconjugates
Polyurethanes
Spectrometry, Fluorescence
Spectroscopy, Fourier Transform Infrared
Trypsin

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22413358