Abstract
| 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 Sep 2016 |
| DOIs | |
| Publication status | Published - 15 Feb 2017 |
Fingerprint
Cite this
}
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; Bremner, David H.; Hungerford, Graham.
In: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, Vol. 173, 15.02.2017, p. 324-327.Research output: Contribution to journal › Article
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
VL - 173
SP - 324
EP - 327
JO - Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
JF - Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
SN - 1873-3557
ER -