Interfacial behavior of Lactate Oxidase at Air-Subphase interface

Marystela Ferreira, Shiv K. Sharma, Suraj Paudyal, Roger M. Leblanc

Research output: Contribution to journalArticlepeer-review

Abstract

This article investigates the main aspects of the surface chemistry properties of the lactate oxidase (LacOx) enzyme monolayer at the air-subphase interface. Surface chemistry study determined the important properties like the surface packing and stability of the formed layer, whereas the spectroscopic experiments provided information regarding its secondary structure conformation of the enzyme. We have demonstrated that the LacOx in the monolayer form remained active for extended time period. In accordance to the data obtained from the isotherm it was also found that LacOx forms a stable monolayer that does not aggregate at the air-subphase interface. The stability of the monolayer at the air-subphase interface was studied by using compression-decompression cycles which revealed the stability with no significant evidence of aggregates or irreversible domains. This was further confirmed by UV–vis absorption and fluorescence measurements. Spectra from circular dichroism (CD) showed that the LB film retains the characteristic of an α-helix conformation.

Original languageEnglish (US)
Pages (from-to)173-178
Number of pages6
JournalJournal of Colloid And Interface Science
Volume589
DOIs
StatePublished - May 2021

Keywords

  • Lactate oxidase
  • Langmuir monolayer
  • Langmuir-Blodgett film
  • Spectroscopy
  • Surface chemistry

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Biomaterials
  • Surfaces, Coatings and Films
  • Colloid and Surface Chemistry

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