Pulsed Electric Field: Fundamentals and Effects on the Structural and Techno-Functional Properties of Dairy and Plant Proteins
Abstract
:1. Introduction
2. PEF vs. Other Processing Technologies
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- Short processing times;
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- Waste-free process;
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- Low energy consumption;
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- Environmentally-friendly technique;
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- Better retention of nutrients, flavors, and colors; and
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- Suitability for processing heat-sensitive foods.
Processing Technology | Processing Parameters | Mechanism | Effects on Protein Structure | Effects on Proteins’ Techno-Functional Properties |
---|---|---|---|---|
PEF | Pulse-wave shape, pulse duration, electric field strength, frequency, temperature, and treatment duration [68]. | Polarization of protein molecules and release of free radicals can induce changes in protein structures and functionalities [4]. | Depends on the electric field strength and the type of proteins. Main changes occurred in the secondary structure and exposure of hydrophobic groups to the surface of protein molecules [33]. | Different waveforms and protein types can have different effects on protein solubility. Emulsifying and foaming properties improved [69]. |
Ultrasound | Amplitude, frequency, acoustic energy, intensity, energy density (J/mL), time, and temperature [70]. | Acoustic cavitation (the formation and collapse of air bubbles) induces chemical reactions and physical effects, which influence the structure and techno-functional properties of proteins [71]. | Changes in the secondary and tertiary structures. Increases in surface hydrophobicity and free sulfhydryl groups [51] | Ultrasound improved the emulsifying and gelling properties of proteins [72]. |
High pressure processing | Pressure, temperature, and time [53] | Protein unfolding can occur due to the penetration of water into the protein matrix [38]. | Depends on the applied conditions and protein system. Mainly protein denaturation and aggregation occurred [73]. | Depends on the applied pressure. Emulsifying and foaming capabilities enhanced. Solubility of proteins improved [74]. |
Microwave | Power, frequency, time, and temperature [56]. | At the molecular level, exposed proteins interact with electromagnetic energy. Then, heat is generated from the electromagnetic energy through the motion of molecules during treatment [71]. | Changes in the secondary structure. Protein aggregation [75]. | Gelling properties improved [76]. |
Cold-plasma processing | Voltage, frequency, time, and temperature [77]. | Several high-energy radicals, such as nitric oxide, atomic oxygen, superoxide, and hydroxyl radicals to break the covalent bonds and promote several chemical reactions [78]. | The high-energy reaction could break peptide bonds and oxidize the side chains of amino acids. They may also facilitate the formation of protein–protein interactions. Changes in the secondary structures were observed [61]. | Water- and oil-holding capacities enhanced, reflecting the improvement of emulsifying and gelling properties of proteins [62]. |
3. Fundamentals of PEF Technology: Device Components and Pulse Generation
4. Effects of PEF on the Structure of Dairy and Plant Proteins
5. Effects of PEF on the Techno-Functional Properties of Dairy and Plant Proteins
5.1. Protein Solubility
5.2. Gelling Properties
5.3. Emulsifying and Foaming Properties
6. Conclusions and Future Perspectives
- In general, PEF treatment at low electric strength (<10 kV/cm) cannot change the structure of proteins;
- PEF treatment conditions, such as electric strength, pulse shape, pulse duration, and the type of treatment chamber, have a significant impact on the effects of PEF on the structure and techno-functional properties of proteins’
- The effects of PEF on structure and techno-functional properties are vary from one protein type to another.
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Conflicts of Interest
References
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Component | Description and Function(s) | References |
---|---|---|
High-voltage pulse generator |
| [80] |
Resistors | Delay the current flow and impose a voltage reduction. | [83] |
Capacitors | Energy (voltage) storage. | [84] |
Switchers | Connect or disconnect the electric current and control the discharge of the stored energy. | [20] |
Treatment chambers | Specific containers are used to carry food samples during exposure to PEF. | [81,85] |
Dairy Protein | PEF Conditions | Structural Changes | References |
---|---|---|---|
Whey protein | 35.5 kV/cm for 300 or 1000 µs, pulse duration of 7 µs, and pulse repetition rate set at 111 Hz. | Significant differences in the concentration of α-LA, β-LG, and serum albumin between PEF-treated samples for 300 µs and 1000 µs. | [100] |
Whey protein isolate (WPI) | 12, 16, and 20 kV/cm; number of pulses (10, 20, and 30) |
| [22] |
WPI | 30–35 kV/cm, 19.2–211 µs, 30–75 °C, flow rate of 60 mL/min |
| [95] |
Lactoferrin | Intensity of 35 kV/cm, pulse width of 2 µs, and pulse frequency of 200 or 100 Hz.; flow rate of 60 mL/min. |
| [24] |
β-lactoglobulin | Intensity of 12.5 kV/cm with 40 µF of capacitance. 1–10 pulses, with 15 s between pulses. | PEF partially denatured β-lactoglobulin. | [31] |
Whole milk | Intensity of 20 or 26 kV/cm for 34 µs, bipolar square wave pulses, pulse width of 20 µs for 34 μs. | The surface hydrophobicity of milk proteins increased with increased electric field intensity. | [97] |
Sodium caseinate | 10–150 V/cm for 5 s—2 h using a 60 Hz sine wave alternating current. | Moderate electric field altered the secondary structure of sodium caseinate and unfolded the protein molecules. | [33] |
β-lactoglobulin | 20 V/cm during holding and 80 V/cm during heating at a frequency of 20 kHz for 5–7 min. | Changes in the secondary structure of β-lactoglobulin. | [99] |
Bovine serum albumin (BSA) | Strengths of 78, 150, 300, and 500 V/m for 3 h. | Low-intensity electric field changed the tertiary structure of BSA. | [96] |
Plant Protein | PEF Conditions | Structural Changes | References |
---|---|---|---|
Soy protein isolate (SPI) | 0–40 kV/cm for 0–547 μs, 2 ms pulse width, and 500 pulse per second (pps) pulse frequency. |
| [29] |
SPI | 0 to 50 kV/cm, 40 μs pulse width, 1.0 kHz frequency, and 10 mL/min flow speed. |
| [101] |
Sunflower protein | 10–150 V/cm for 5 s-2 h at 25–45 °C. |
| [33] |
Canola protein | 10 to 35 kV, pulse frequency of 600 Hz, and pulse width of 8 μs. |
| [69] |
Pea protein isolate | 5, 10, and 20 V/cm and frequencies of 50 Hz and 20 kHz. |
| [102] |
Dairy Protein | PEF Conditions | Changes in Protein Functionality | References |
---|---|---|---|
Raw milk | Intensity of 30 kV/cm, outlet temperature of 50 ± 1 °C; pulse number of 80 and 120 pulses, pulse width of 2 µs, and pulse frequency of 2 Hz. | Rennet coagulation time (RCT) higher than that of raw milk but lower than that of pasteurized milk. | [105] |
Whey protein isolate (WPI) | 15–22 V/cm heating phase and 4 to 8 V/cm holding phase, frequency of 25 kHz. | Moderate electric field treatment resulted in a weaker gel structure than conventional heat treatment. | [106] |
β-lactoglobulin | 20 V/cm during holding, 80 V/cm during heating, and frequency of 20 kHz. | At pH 7, moderate electric field and thermal treatment (up to 60 °C) had similar effects on the free SH group relativity. At higher temperatures, conventional heat-treated samples had higher free-SH-group relativity than moderate electric field-treated samples. | [99] |
WPI | 30–35 kV/cm, 19.2–211 µs, 30–75 °C. |
| [95] |
β-lactoglobulin | Intensity of 12.5 kV/cm with 40 µF of capacitance. | PEF improved the gelling rate of β-lactoglobulin (at 72 °C) when the number of pulses was less than six. | [31] |
WPI | 15 to 55 kV/cm, 2 to 8 and 50 to 90 °C. | The gelling properties of WPI increased when treated at 35 kV/cm but decreased after treatment at 45 kV/cm. | [107] |
Plant Protein | PEF Conditions | Changes in Protein Functionality | References |
---|---|---|---|
Soy protein isolate (SPI) | 0–40 kV/cm for 0–547 μs, 2 ms pulse width, and 500 pulse per second (pps) pulse frequency. |
| [29] |
Canola protein | 10 to 35 kV, pulse frequency of 600 Hz, and pulse width of 8 μs. |
| [69] |
Sunflower protein | 10–150 V/cm for 5 s–2 h at 25–45 °C. |
| [33] |
Pea protein isolate | 5, 10, and 20 V/cm and frequencies of 50 Hz and 20 kHz. |
| [102] |
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Taha, A.; Casanova, F.; Šimonis, P.; Stankevič, V.; Gomaa, M.A.E.; Stirkė, A. Pulsed Electric Field: Fundamentals and Effects on the Structural and Techno-Functional Properties of Dairy and Plant Proteins. Foods 2022, 11, 1556. https://doi.org/10.3390/foods11111556
Taha A, Casanova F, Šimonis P, Stankevič V, Gomaa MAE, Stirkė A. Pulsed Electric Field: Fundamentals and Effects on the Structural and Techno-Functional Properties of Dairy and Plant Proteins. Foods. 2022; 11(11):1556. https://doi.org/10.3390/foods11111556
Chicago/Turabian StyleTaha, Ahmed, Federico Casanova, Povilas Šimonis, Voitech Stankevič, Mohamed A. E. Gomaa, and Arūnas Stirkė. 2022. "Pulsed Electric Field: Fundamentals and Effects on the Structural and Techno-Functional Properties of Dairy and Plant Proteins" Foods 11, no. 11: 1556. https://doi.org/10.3390/foods11111556