Issue 33, 2015

Charge-switchable gold nanoparticles for enhanced enzymatic thermostability

Abstract

This study illustrates a facile strategy for efficient immobilization of enzymes on a metal nanoparticle surface. The strategy proposed here enables the enzymatic activity to be retained while increasing the enzyme thermostability. It is demonstrated that the use of a zwitterionic amino acid tyrosine as a reducing and capping agent to synthesise gold nanoparticles allows efficient immobilization of phytase enzyme through charge-switchable electrostatic interactions. The detailed kinetic and thermodynamic studies reveal that the proposed enzyme immobilization strategy improves the overall quality of phytase by reducing the activation energy required for substrate hydrolysis and broadening the temperature window in which immobilized enzyme is able to operate. The outcomes of this study indicate that the underlying zwitterionic nature of 20 natural amino acids along with significant variability in their isoelectric points and hydropathy indices as well the ability of some of the amino acids to reduce metal ions is likely to offer significant opportunities for tailoring nano-bio interfaces in a rational manner for a range of biological applications.

Graphical abstract: Charge-switchable gold nanoparticles for enhanced enzymatic thermostability

Supplementary files

Article information

Article type
Paper
Submitted
26 May 2015
Accepted
13 Jul 2015
First published
16 Jul 2015

Phys. Chem. Chem. Phys., 2015,17, 21517-21524

Author version available

Charge-switchable gold nanoparticles for enhanced enzymatic thermostability

S. Shankar, S. K. Soni, H. K. Daima, P. R. Selvakannan, J. M. Khire, S. K. Bhargava and V. Bansal, Phys. Chem. Chem. Phys., 2015, 17, 21517 DOI: 10.1039/C5CP03021H

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