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

doi:10.1016/j.saa.2016.09.035

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 journal › Article › peer-review

8 Citations (Scopus)

237 Downloads (Pure)

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 language	English
Pages (from-to)	324-327
Number of pages	4
Journal	Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
Volume	173
Early online date	20 Sept 2016
DOIs	https://doi.org/10.1016/j.saa.2016.09.035
Publication status	Published - 15 Feb 2017

Keywords

High frequency ultrasound
Time-resolved emission spectrum
Decay associated spectra
Excitation-emission matrix
Metal catalysed oxidation

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10.1016/j.saa.2016.09.035

Tsikrika_TimeResolvedFluorescenceObservation_Accepted_2016Accepted author manuscript, 159 KBLicence: CC BY-NC-ND

Boon Chu
- boon-seang.chuabertay.acuk
- Department of Built Environment and Life Sciences - Reader in Food Functionality and Processing Technology
Person: Academic
Adilia Lemos
- a.lemosabertay.acuk
- Abertay University - Faculty International and Partnership Lead
- Department of Built Environment and Life Sciences - Lecturer
Person: Academic

Effect of high and how frequency ultrasound on foods (enzyme activity, polyphenolic compounds and antioxidant activity)
Lemos, A. (Contributor), Chu, B. (Contributor), Tsikrika, K. (Contributor), Bremner, D. (Contributor) & Hungerford, G. (Contributor), Mendeley Data, 24 Jun 2022
DOI: 10.17632/n4f6hc8757.1
Dataset

Cite this

@article{7f8014d8046542f3a6c1fb02807eaeaa,

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

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.",

author = "Konstantina Tsikrika and Lemos, \{M. Adilia\} and Boon-Seang Chu and Bremner, \{David H.\} and Graham Hungerford",

year = "2017",

month = feb,

day = "15",

doi = "10.1016/j.saa.2016.09.035",

language = "English",

volume = "173",

pages = "324--327",

journal = "Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy",

issn = "1873-3557",

}

Time-resolved fluorescence observation of di-tyrosine formation in horseradish peroxidase upon ultrasound treatment leading to enzyme inactivation. / Tsikrika, Konstantina; Lemos, M. Adilia ; Chu, Boon-Seang et al.
In: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, Vol. 173, 15.02.2017, p. 324-327.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Time-resolved fluorescence observation of di-tyrosine formation in horseradish peroxidase upon ultrasound treatment leading to enzyme inactivation

AU - Tsikrika, Konstantina

AU - Lemos, M. Adilia

AU - Chu, Boon-Seang

AU - Bremner, David H.

AU - Hungerford, Graham

PY - 2017/2/15

Y1 - 2017/2/15

N2 - 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.

AB - 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.

U2 - 10.1016/j.saa.2016.09.035

DO - 10.1016/j.saa.2016.09.035

M3 - Article

SN - 1873-3557

VL - 173

SP - 324

EP - 327

JO - Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy

JF - Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy

ER -

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

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Adilia Lemos

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Effect of high and how frequency ultrasound on foods (enzyme activity, polyphenolic compounds and antioxidant activity)

Cite this