The Protein Journal

, Volume 34, Issue 5, pp 329–337 | Cite as

Conformational Change Results in Loss of Enzymatic Activity of Jack Bean Urease on Its Interaction with Silver Nanoparticle

  • Shobana Ponnuvel
  • Balakumar Subramanian
  • Karthe Ponnuraj
Article
First Online:

Abstract

Urease is an enzyme produced by microbes such as bacteria, yeast and fungi. Plants also produce this enzyme. Urease action splits urea into ammonia and carbamate. This action is having important implications in agro-chemical, medicinal and environment. Therefore there is always a constant search for new and novel compounds which could inhibit this enzyme. Here we have studied the interaction of jack bean urease (JBU) with silver nanoparticle to analyze the influence of the resultant protein corona formation on the catalytic property of JBU. Several techniques like UV–Vis, gel shift assay and CD spectroscopy have been used to characterize this interaction. Urease activity assay suggests that the protein corona formation inhibits the enzymatic action of JBU. The loss of enzymatic action could be either due to the nanoparticle blocking the active site of JBU or a conformational change in the protein. The CD spectra of JBU–AgNP complexes clearly revealed significant changes in the secondary structural composition of the JBU and this could be the reason for the loss of enzymatic activity of JBU. This study revealed an interesting observation, where the interaction of AgNP with JBU resulted destabilization of hexameric nature of JBU which is otherwise highly stable. The results of the present study could be useful in the development of nanoparticle based material for inhibiting the ureolytic activity of ureases in different fields.

Keywords

Jack bean urease (JBU) Silver nanoparticle (AgNP) Enzyme-nanoparticle corona Circular dichroism (CD) Conformational change 

Abbreviations

PDB

Protein Data Bank

JBU

Jack bean urease

AgNP

Silver nanoparticle

SDS-PAGE

Sodium dodecyl sulphate polyacrylamide gel electrophoresis

CD

Circular dichroism

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Notes

Acknowledgments

KP and SP thank National Centre for Nanoscience and Nanotechnology (NCNSNT), University of Madras, India for financial support in the form of research grant and fellowship respectively.

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Copyright information

© Springer Science+Business Media New York 2015

Authors and Affiliations

  • Shobana Ponnuvel
    • 1
  • Balakumar Subramanian
    • 2
  • Karthe Ponnuraj
    • 1
  1. 1.Centre of Advanced Study in Crystallography and BiophysicsUniversity of MadrasChennaiIndia
  2. 2.National Centre for Nanoscience and NanotechnologyUniversity of MadrasChennaiIndia

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