Ohmic Heating in Food Processing: An Overview of Plant-Based Protein Modification
Abstract
:1. Introduction
2. Ohmic Heating
3. Ohmic Heating Applied to Food Proteins
Protein | Experimental Process | Ohmic Heating Treatment | Highlight | References |
---|---|---|---|---|
Soy protein isolate | They assessed the effects of ohmic and conventional heating on structural, thermal, and physical changes in soy protein isolate edible films. | The electrical frequency for treatment was 50 Hz, and the electric field intensities used for ohmic treatment were 3, 6, 9, and 12 V·cm−1, compared to conventional heating. | Ohmic-heated films exhibited reduced α-helix content, increased random coil content, smaller average particle size, lower fluorescence intensity, and higher surface hydrophobicity. | [36] |
Sunflower protein isolate | They analyzed the structural, thermal, and physical changes in sunflower protein isolate compared to sodium caseinate when subjected to the application of non-thermal moderate electric field (MEF). | Electric field application: sample had 10 V/cm for 1 h (V1) and 10 V/cm for 2 h (V2) applied; sample had 150 V/cm for 5 s (V5) and 150 V/cm for 20 s (V20) applied. | Greater homogeneity was achieved with V20. The secondary and tertiary structures of sunflower protein changed primarily with V20, gaining a bulkier and more flexible structure and increased surface hydrophobicity. V5 had the lowest denaturation enthalpy. V1 also produced sodium caseinate solution with the lowest denaturation enthalpy. | [10] |
Soy protein isolate | They studied the effect of ohmic heating on the structure and immunoreactive properties of soy proteins. | Ohmic heating studies were conducted at various frequencies, including 50 Hz, 500 Hz, 2 kHz, and 20 kHz. The electrode distance was consistently maintained at 30 mm for all assessed conditions. When necessary, the electric field intensities during the procedure ranged from 2 V/cm to 20 V/cm. Soybean trypsin inhibitor allergenic protein (STI), also known as Gly m TI, was selected as the allergen of interest due to its remarkable resistance to thermal treatments | Ohmic heating applications at frequencies ranging from 50 to 500 Hz can lead to conformational changes in soy protein fractions, as evidenced by the reduced fluorescence of aromatic amino acids. This effect may be directly associated with the formation of complexes with metals present in the protein solution during ohmic heating. However, there is a lack of detailed information on how electrical variables, such as electric field and frequency, affect soy protein fractions in this specific context. | [31] |
Lactoferrin | The purpose of study was to create gel-like gelatin emulsions using lactoferrin dispersions heated through ohmic treatment. The impact of both ohmic and conventional heating on the protein’s secondary structure and the subsequent thermal aggregation of lactoferrin was assessed. | Ohmic heating was applied using a 4 cm electrode gap, with voltages ranging from 36 to 86 V. This treatment was compared to conventional heating. A double-walled glass reactor vessel was used, and a 20 mL lactoferrin dispersion was heated to 90 °C for 30 min for both treatments. | Both ohmic and conventional heating influenced the thermal unfolding and aggregation of lactoferrin molecules. Ohmic heating likely affected the molecular flexibility or the stability of lactoferrin’s hydrophobic groups. Ohmic heating resulted in fewer aggregated protein molecules compared to conventional heating. The difference in aggregation patterns was confirmed by a smaller increase in particle size, turbidity, intrinsic and extrinsic fluorescence, and a distinct dichroic signal, impacting the structural and mechanical properties of the prepared emulsions. | [37] |
β—Lactoglobulin | They investigated the effect of moderate electric fields (MEF) during the ohmic heating of purified β-lactoglobulin fractions under different physicochemical conditions of pH and temperature. | The treatments were conducted at temperatures of 50, 60, 70, 80, and 90 °C for 10 min. The applied electric field intensity varied from 80 V/cm during the heating phase to 20 V/cm during the holding step. The electric frequency remained constant at 20 kHz, as the choice of frequencies within the kHz range was adopted to prevent unwanted electrochemical effects, such as electrolysis and electrode oxidation. | The results indicated that the effects of moderate electric field (MEF) are limited to unfolded protein conformations. This suggests that under the specific conditions tested, including electric field intensity, frequency, and exposure period, the imposed disturbances are not significant enough to impede the protein folding process. Thus, the effects of MEF appear to act synergistically with thermal effects. Furthermore, their specific influence and scope varied according to the pH, which may be related to the flexibility of β-lactoglobulin in response to environmental conditions. These findings support theories presented in other studies, which had already demonstrated that moderate electric field (MEF) effects impact the aggregation and gelation of serum proteins. | [38] |
Whey protein isolate | They evaluated the formation of soluble whey protein aggregates from whey protein isolated under conditions of near-neutral pH, both in the presence and absence of a moderate electric field (MEF). | The applied voltage and temperature were controlled using a function generator connected to an amplifier system. During the heating and holding phases, the applied voltage ranged from 15 to 22 V/cm and 4 to 8 V/cm, respectively. The electrical frequency was 25 kHz, chosen to reduce electrochemical reactions at the electrode interface, minimizing the potential for corrosion and metal leakage into the medium. The results were compared to conventional heating. | The results indicated that the application of moderate electric fields impacts the unfolding and aggregation processes of whey protein at relatively high temperatures. After heating at 85 °C for 30 s, treatments with moderate electric fields resulted in whey protein isolate solutions with a higher amount of β-Lactoglobulin (8%) and α-Lactalbumin (10%) in their native form, compared to a traditional heating method. The protein aggregates in solutions treated with a moderate electric field increased by up to 78 nm, while conventional heating led to an 86 nm increase in the size of these aggregates. The aggregation of whey proteins under the influence of the moderate electric field was not intense enough to create an elastic gel network. This is due to reductions in the value of storage and loss moduli after treatment with the moderate electric field. | [39] |
Lentil protein isolate | They assessed the impact of ohmic heating (temperature, electric field intensity, and frequency) on the structure of lentil protein obtained through alkaline extraction and protein–pectin interactions | The heating was conducted at temperatures of 40, 50, 60, 70, and 80 °C. After reaching the desired temperature, a waiting period of 30 s was observed. The voltages used for heating and maintaining a constant temperature were 5 and 75 V/cm, respectively. In the ohmic heating treatments, the initial phase involved the application of an electric field of 75 V/cm until the solution reached 80 °C. In the first ohmic treatment, the voltage was reduced to 5 V/cm, and the temperature was kept constant at 80 °C. In the second treatment (OH-75 V/cm), electric fields ranging from 10 to 20 V/cm were used while maintaining the temperature at 80 °C. | The results indicated that the characteristics of lentil protein were modified by the thermal processes, with the extent of these modifications being influenced by the treatment temperature, electric field intensity, and pH during protein fraction extraction. Lentil protein extracted at pH 9 showed greater stability to temperature variations during ohmic heating. Under low electric field conditions (5 V/cm), there was an increase in protein surface hydrophobicity and accessibility to sulfhydryl groups. In contrast, lentil protein extracted at pH 7 was significantly affected by all thermal treatments. While some structural changes were observed in specific protein characteristics, no influences on protein–pectin interactions in lentil were identified. | [40] |
3.1. Ohmic Heating in Coagulated Products
3.2. Thermal Treatment Using Ohmic Heating to Improve Protein Stability and Protein–Molecule Interactions
3.3. Effect on Chemical Bonds
3.4. Techno-Functional Properties
3.4.1. Water-Holding Capacity and Solubility
3.4.2. Oil-Holding Capacity and Emulsification
3.4.3. Gelling Properties
4. Final Considerations
Author Contributions
Funding
Conflicts of Interest
References
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Advantages | Disadvantages |
---|---|
Fast and uniform heating: Ohmic heating can heat food quickly and evenly, preventing hot and cold spots. This helps maintain the quality of the final product. | High initial costs: The installation of ohmic heating equipment can be expensive, which can be a barrier for small food processing businesses. |
Energy efficiency: Compared to some conventional heating methods, ohmic heating can be more energy-efficient as it directly converts electricity into heat in the food. | Potential quality issues: Depending on the food composition and processing conditions, ohmic heating can affect the texture, color, and taste of food undesirably. Another concern is the migration of metallic ions from the electrodes into the food. |
Precise temperature control: Precise temperature control during ohmic heating is possible, which is important for ensuring food safety and the quality of the final product. | Requires conductive foods: Ohmic heating works best with foods that are good electrical conductors. Foods with low electrical conductivity (such as those high in fats) may be less effective in this process. |
Reduced nutrient loss: In some cases, ohmic heating may result in less nutrient loss compared to more aggressive thermal processing methods, such as prolonged boiling. This can be achieved thanks to more uniform and rapid heating, which allows for reduced temperature and shorter exposure time of the food to heat. Additionally, the food is heated directly through the passage of electrical current, eliminating the need for heating mediums such as water, which can lead to nutrient loss through leaching. | Need for technical monitoring: Due to the precision required in temperature control, ohmic heating processes demand constant technical monitoring, which can increase operational costs. |
Reduced need for additives: Since the process is quick and effective in reducing microorganisms, there may be a reduced need for chemical additives or preservatives. Additionally, the reduced exposure of the food to heat minimizes thermal damage to the food matrix, which decreases the need for added additives to compensate for sensory loss caused by heating. | Potential for electrical burns: There is a risk of electrical shock when using ohmic heating equipment, necessitating the implementation of appropriate safety measures |
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dos Santos, I.F.; Pimentel, T.C.; da Cruz, A.G.; Stringheta, P.C.; Martins, E.; Campelo, P.H. Ohmic Heating in Food Processing: An Overview of Plant-Based Protein Modification. Processes 2024, 12, 1800. https://doi.org/10.3390/pr12091800
dos Santos IF, Pimentel TC, da Cruz AG, Stringheta PC, Martins E, Campelo PH. Ohmic Heating in Food Processing: An Overview of Plant-Based Protein Modification. Processes. 2024; 12(9):1800. https://doi.org/10.3390/pr12091800
Chicago/Turabian Styledos Santos, Israel Felipe, Tatiana Colombo Pimentel, Adriano Gomes da Cruz, Paulo César Stringheta, Evandro Martins, and Pedro Henrique Campelo. 2024. "Ohmic Heating in Food Processing: An Overview of Plant-Based Protein Modification" Processes 12, no. 9: 1800. https://doi.org/10.3390/pr12091800