Monatshefte für Chemie - Chemical Monthly

, Volume 149, Issue 11, pp 2131–2136 | Cite as

Investigating the MgO nanoparticles and trypsin interaction through spectroscopic methods

  • Sheida Mahmodian
  • Lida Momeni
  • Behzad ShareghiEmail author
Original Paper


The aim of this work was to study the effect of MgO nanoparticles (NPs) on both the structure and activity of the trypsin enzyme at pH 8.0 using UV–Vis spectroscopy, fluorescence spectroscopy, and enzyme activity assay techniques. The examination of the enzyme activity revealed that the MgO-NPs tended to increase the latter. Moreover, it was found that the rise in the trypsin UV–Vis absorption could be due to the formation of the trypsin–MgO-NPs complexes. The Stern–Volmer constant was reduced as the temperature was increased from 298 to 308 K, thereby indicating that the MgO-NPs caused the intrinsic fluorescence quench of trypsin via the static quenching mechanism. Furthermore, the detailed analysis of thermodynamic parameters for our fluorescence data revealed the spontaneous binding of trypsin to the MgO-NPs, with the hydrogen bonding and van der Waals interactions being only the main physical basis of the trypsin–MgO-NPs coupling.

Graphical abstract


Trypsin Fluorescence Enzyme Activity 


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Copyright information

© Springer-Verlag GmbH Austria, part of Springer Nature 2018

Authors and Affiliations

  • Sheida Mahmodian
    • 1
  • Lida Momeni
    • 2
  • Behzad Shareghi
    • 1
    Email author
  1. 1.Department of Biology, Faculty of ScienceShahrekord UniversityShahrekordIran
  2. 2.Department of Biology, Faculty of SciencePayam Noor UniversityTehranIran

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