Effect of tin oxide nanoparticle binding on the structure and activity of α-amylase from Bacillus amyloliquefaciens

Mohammad Jahir Khan, Shariq Qayyum, Fahad Alam, Qayyum Husain

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


Proteins adsorbed on nanoparticles (NPs) are being used in biotechnology, biosensors and drug delivery. However, understanding the effect of NPs on the structure of proteins is still in a nascent state. In the present paper tin oxide (SnO2) NPs were synthesized by the reaction of SnCl 45H2O in methanol via the sol-gel method and characterized by x-ray diffraction (XRD), Fourier transform infrared spectroscopy (FT-IR) and transmission electron microscopy (TEM). The binding of these SnO 2-NPs with α-amylase was investigated by using UV-vis, fluorescence and circular dichroism (CD) spectroscopic techniques. A strong quenching of tryptophan fluorescence intensity in α-amylase was observed due to formation of a ground state complex with SnO2-NPs. Far-UV CD spectra showed that the secondary structure of α-amylase was changed in the presence of NPs. The Michaelis-Menten constant (Km), was found to be 26.96 and 28.45mgml- 1, while Vmax was 4.173 and 3.116mgml- 1min- 1 for free and NP-bound enzyme, respectively. © 2011 IOP Publishing Ltd.
Original languageEnglish (US)
Issue number45
StatePublished - Nov 11 2011
Externally publishedYes

Bibliographical note

Generated from Scopus record by KAUST IRTS on 2023-09-23

ASJC Scopus subject areas

  • Bioengineering
  • Mechanics of Materials
  • General Materials Science
  • General Chemistry
  • Mechanical Engineering
  • Electrical and Electronic Engineering


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