Time-resolved fluorescence observation of di-tyrosine formation in horseradish peroxidase upon ultrasound treatment leading to enzyme inactivation

Konstantina Tsikrika, M. Adilia Lemos, Boon-Seang Chu, David H. Bremner, Graham Hungerford*

*Corresponding author for this work

    Research output: Contribution to journalArticle

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    Abstract

    The application of ultrasound to a solution can induce cavitional phenomena and generate high localised temperatures and pressures. These are dependent of the frequency used and have enabled ultrasound application in areas such as synthetic, green and food chemistry. High frequency (100 kHz to 1 MHz) in particular is promising in food chemistry as a means to inactivate enzymes, replacing the need to use periods of high temperature. A plant enzyme, horseradish peroxidase, was studied using time-resolved fluorescence techniques as a means to assess the effect of high frequency (378 kHz and 583 kHz) ultrasound treatment at equivalent acoustic powers. This uncovered the fluorescence emission from a newly formed species, attributed to the formation of di-tyrosine within the horseradish peroxidase structure caused by auto-oxidation, and linked to enzyme inactivation.
    Original languageEnglish
    Pages (from-to)324-327
    Number of pages4
    JournalSpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
    Volume173
    Early online date20 Sep 2016
    DOIs
    Publication statusPublished - 15 Feb 2017

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