Effects of Pulsed Electric Field on the Physicochemical and Structural Properties of Micellar Casein
Abstract
:1. Introduction
2. Materials and Methods
2.1. Materials
2.2. PEF Treatment
2.3. Particle Size and ζ-Potential
2.4. Turbidity
2.5. Protein Solubility
2.6. Surface Hydrophobicity (Ho)
2.7. Intrinsic Fluorescence Spectroscopy
2.8. Scanning Electron Microscopy (SEM)
2.9. Fourier Transform Infrared Spectroscopy (FTIR)
2.10. Raman Spectroscopy
2.11. Statistical Analysis
3. Results and Discussion
3.1. PEF Effects on the Particle Size and ζ-Potential
3.2. Protein Solubility and Turbidity
3.3. Tertiary Structure and Surface Hydrophobicity (Ho)
3.4. Microstructure
3.5. Secondary Structure
3.6. Raman Spectroscopy Analysis
4. Conclusions
Author Contributions
Funding
Data Availability Statement
Acknowledgments
Conflicts of Interest
References
- Jambrak, A.R.; Mason, T.J.; Lelas, V.; Herceg, Z.; Herceg, I.L. Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions. J. Food Eng. 2008, 86, 281–287. [Google Scholar] [CrossRef]
- Wagoner, T.; Vardhanabhuti, B.; Foegeding, E.A. Designing Whey Protein–Polysaccharide Particles for Colloidal Stability. Annu. Rev. Food Sci. Technol. 2016, 7, 93–116. [Google Scholar] [CrossRef] [PubMed]
- Goulding, D.A.; Fox, P.F.; O’Mahony, J.A. Milk Proteins: An Overview. In Milk Proteins: From Expression to Food; Academic Press: Cambridge, MA, USA, 2020; pp. 21–98. ISBN 9780128152515. [Google Scholar]
- Nunes, L.; Tavares, G.M. Thermal treatments and emerging technologies: Impacts on the structure and techno-functional properties of milk proteins. Trends Food Sci. Technol. 2019, 90, 88–99. [Google Scholar] [CrossRef]
- Rahman, M.; Lamsal, B.P. Ultrasound-assisted extraction and modification of plant-based proteins: Impact on physicochemical, functional, and nutritional properties. Compr. Rev. Food Sci. Food Saf. 2021, 20, 1457–1480. [Google Scholar] [CrossRef] [PubMed]
- Xue, S.; Xu, X.; Shan, H.; Wang, H.; Yang, J.; Zhou, G. Effects of high-intensity ultrasound, high-pressure processing, and high-pressure homogenization on the physicochemical and functional properties of myofibrillar proteins. Innov. Food Sci. Emerg. Technol. 2018, 45, 354–360. [Google Scholar] [CrossRef]
- Munir, M.; Nadeem, M.; Qureshi, T.M.; Leong, T.S.; Gamlath, C.J.; Martin, G.J.; Ashokkumar, M. Effects of high pressure, microwave and ultrasound processing on proteins and enzyme activity in dairy systems—A review. Innov. Food Sci. Emerg. Technol. 2019, 57, 102192. [Google Scholar] [CrossRef]
- Heinz, V.; Toepfl, S. Pulsed Electric Fields Industrial Equipment Design. Food Eng. Ser. 2022, 489–504. [Google Scholar] [CrossRef]
- Arshad, R.N.; Abdul-Malek, Z.; Munir, A.; Buntat, Z.; Ahmad, M.H.; Jusoh, Y.M.; Bekhit, A.E.-D.; Roobab, U.; Manzoor, M.F.; Aadil, R.M. Electrical systems for pulsed electric field applications in the food industry: An engineering perspective. Trends Food Sci. Technol. 2020, 104, 1–13. [Google Scholar] [CrossRef]
- Buckow, R.; Ng, S.; Toepfl, S. Pulsed Electric Field Processing of Orange Juice: A Review on Microbial, Enzymatic, Nutritional, and Sensory Quality and Stability. Compr. Rev. Food Sci. Food Saf. 2013, 12, 455–467. [Google Scholar] [CrossRef]
- Xiang, B.Y.; Ngadi, M.O.; Ochoa-Martinez, L.A.; Simpson, M.V. Pulsed Electric Field-Induced Structural Modification of Whey Protein Isolate. Food Bioprocess Technol. 2009, 4, 1341–1348. [Google Scholar] [CrossRef]
- Wang, Q.; Wei, R.; Hu, J.; Luan, Y.; Liu, R.; Ge, Q.; Yu, H.; Wu, M. Moderate pulsed electric field-induced structural unfolding ameliorated the gelling properties of porcine muscle myofibrillar protein. Innov. Food Sci. Emerg. Technol. 2022, 81. [Google Scholar] [CrossRef]
- Liu, Y.Y.; Zeng, X.A.; Deng, Z.; Yu, S.J.; Yamasaki, S. Effect of pulsed electric field on the secondary structure and thermal properties of soy protein isolate. Eur. Food Res. Technol. 2011, 233, 841–850. [Google Scholar] [CrossRef]
- 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. [Google Scholar] [CrossRef] [PubMed]
- Sui, Q.; Roginski, H.; Williams, R.P.; Versteeg, C.; Wan, J. Effect of pulsed electric field and thermal treatment on the physicochemical and functional properties of whey protein isolate. Int. Dairy J. 2011, 21, 206–213. [Google Scholar] [CrossRef]
- Bekard, I.; Dunstan, D.E. Electric field induced changes in protein conformation. Soft Matter 2013, 10, 431–437. [Google Scholar] [CrossRef]
- Rodrigues, R.M.; Avelar, Z.; Vicente, A.A.; Petersen, S.B.; Pereira, R.N. Influence of moderate electric fields in β-lactoglobulin thermal unfolding and interactions. Food Chem. 2020, 304, 125442. [Google Scholar] [CrossRef] [Green Version]
- Rodrigues, R.M.; Fasolin, L.H.; Avelar, Z.; Petersen, S.B.; Vicente, A.A.; Pereira, R.N. Effects of moderate electric fields on cold-set gelation of whey proteins—From molecular interactions to functional properties. Food Hydrocoll. 2020, 101, 105505. [Google Scholar] [CrossRef] [Green Version]
- Onwulata, C.I.; Tunick, M.H.; Qi, P.X. Extrusion Texturized Dairy Proteins. Processing and Application, 1st ed.; Elsevier Inc.: Amsterdam, The Netherlands, 2011; Volume 62, ISBN 9780123859891. [Google Scholar]
- Wu, S.; Li, G.; Xue, Y.; Ashokkumar, M.; Zhao, H.; Liu, D.; Zhou, P.; Sun, Y.; Hemar, Y. Solubilisation of micellar casein powders by high-power ultrasound. Ultrason. Sonochem. 2020, 67, 105131. [Google Scholar] [CrossRef]
- Yang, M.; Zeng, Q.; Wang, Y.; Qin, J.; Zheng, J.; Wa, W. Effect of ultrasound pretreatment on the physicochemical properties and simulated gastrointestinal digestibility of micellar casein concentrates. LWT 2020, 136, 110319. [Google Scholar] [CrossRef]
- Taha, A.; Ahmed, E.; Ismaiel, A.; Ashokkumar, M.; Xu, X.; Pan, S.; Hu, H. Ultrasonic emulsification: An overview on the preparation of different emulsifiers-stabilized emulsions. Trends Food Sci. Technol. 2020, 105, 363–377. [Google Scholar] [CrossRef]
- Ravash, N.; Peighambardoust, S.H.; Soltanzadeh, M.; Pateiro, M.; Lorenzo, J.M. Impact of high-pressure treatment on casein micelles, whey proteins, fat globules and enzymes activity in dairy products: A review. Crit. Rev. Food Sci. Nutr. 2020, 62, 2888–2908. [Google Scholar] [CrossRef]
- Fan, Y.; Yi, J.; Zhang, Y.; Yokoyama, W. Fabrication of curcumin-loaded bovine serum albumin (BSA)-dextran nanoparticles and the cellular antioxidant activity. Food Chem. 2018, 239, 1210–1218. [Google Scholar] [CrossRef] [PubMed]
- Garcia, A.; Alting, A.; Huppertz, T. Effect of sodium hexametaphosphate on heat-induced changes in micellar casein isolate solutions. Int. Dairy J. 2023, 140, 105583. [Google Scholar] [CrossRef]
- Zheng, T.; Li, X.; Taha, A.; Wei, Y.; Hu, T.; Fatamorgana, P.B.; Zhang, Z.; Liu, F.; Xu, X.; Pan, S.; et al. Effect of high intensity ultrasound on the structure and physicochemical properties of soy protein isolates produced by different denaturation methods. Food Hydrocoll. 2019, 97, 105216. [Google Scholar] [CrossRef]
- Taha, A.; Casanova, F.; Šimonis, P.; Jonikaitė-Švėgždienė, J.; Jurkūnas, M.; Gomaa, M.A.; Stirkė, A. Pulsed electric field-assisted glycation of bovine serum albumin/starch conjugates improved their emulsifying properties. Innov. Food Sci. Emerg. Technol. 2022, 82, 103190. [Google Scholar] [CrossRef]
- Xia, W.; Zhu, L.; Delahaije, R.J.; Cheng, Z.; Zhou, X.; Sagis, L.M. Acid-induced gels from soy and whey protein thermally-induced mixed aggregates: Rheology and microstructure. Food Hydrocoll. 2021, 125, 107376. [Google Scholar] [CrossRef]
- Guinee, T.P. Effect of high-temperature treatment of milk and whey protein denaturation on the properties of rennet–curd cheese: A review. Int. Dairy J. 2021, 121, 105095. [Google Scholar] [CrossRef]
- Anema, S.G. Heat-induced changes in caseins and casein micelles, including interactions with denatured whey proteins. Int. Dairy J. 2021, 122, 105136. [Google Scholar] [CrossRef]
- Li, M.; Fokkink, R.; Ni, Y.; Kleijn, J.M. Bovine beta-casein micelles as delivery systems for hydrophobic flavonoids. Food Hydrocoll. 2019, 96, 653–662. [Google Scholar] [CrossRef]
- Wang, H.; Wang, N.; Chen, X.; Wu, Z.; Zhong, W.; Yu, D.; Zhang, H. Effects of moderate electric field on the structural properties and aggregation characteristics of soybean protein isolate. Food Hydrocoll. 2022, 133, 107911. [Google Scholar] [CrossRef]
- Subaşı, B.G.; Jahromi, M.; Casanova, F.; Capanoglu, E.; Ajalloueian, F.; Mohammadifar, M.A. Effect of moderate electric field on structural and thermo-physical properties of sunflower protein and sodium caseinate. Innov. Food Sci. Emerg. Technol. 2021, 67, 102593. [Google Scholar] [CrossRef]
- Jiang, S.; Ding, J.; Andrade, J.; Rababah, T.M.; Almajwal, A.; Abulmeaty, M.M.; Feng, H. Modifying the physicochemical properties of pea protein by pH-shifting and ultrasound combined treatments. Ultrason. Sonochem. 2017, 38, 835–842. [Google Scholar] [CrossRef] [PubMed]
- Shevkani, K.; Singh, N.; Chen, Y.; Kaur, A.; Yu, L. Pulse proteins: Secondary structure, functionality and applications. J. Food Sci. Technol. 2019, 56, 2787–2798. [Google Scholar] [CrossRef] [PubMed]
- Zhu, S.M.; Lin, S.L.; Ramaswamy, H.S.; Yu, Y.; Zhang, Q.T. Enhancement of Functional Properties of Rice Bran Proteins by High Pressure Treatment and Their Correlation with Surface Hydrophobicity. Food Bioprocess Technol. 2016, 10, 317–327. [Google Scholar] [CrossRef]
- Zhao, W.; Yang, R. Pulsed Electric Field Induced Aggregation of Food Proteins: Ovalbumin and Bovine Serum Albumin. Food Bioprocess Technol. 2010, 5, 1706–1714. [Google Scholar] [CrossRef]
- Dong, M.; Xu, Y.; Zhang, Y.; Han, M.; Wang, P.; Xu, X.; Zhou, G. Physicochemical and structural properties of myofibrillar proteins isolated from pale, soft, exudative (PSE)-like chicken breast meat: Effects of pulsed electric field (PEF). Innov. Food Sci. Emerg. Technol. 2019, 59, 102277. [Google Scholar] [CrossRef]
- Wan, Y.; Liu, J.; Guo, S. Effects of succinylation on the structure and thermal aggregation of soy protein isolate. Food Chem. 2018, 245, 542–550. [Google Scholar] [CrossRef]
- Wang, Y.-R.; Yang, Q.; Fan, J.-L.; Zhang, B.; Chen, H.-Q. The effects of phosphorylation modification on the structure, interactions and rheological properties of rice glutelin during heat treatment. Food Chem. 2019, 297, 124978. [Google Scholar] [CrossRef]
- Li, M.; Kong, J.; Chen, Y.; Li, Y.; Xuan, H.; Liu, M.; Zhang, Q.; Liu, J. Comparative interaction study of soy protein isolate and three flavonoids (Chrysin, Apigenin and Luteolin) and their potential as natural preservatives. Food Chem. 2023, 414, 135738. [Google Scholar] [CrossRef]
- Guo, Z.; Huang, Z.; Guo, Y.; Li, B.; Yu, W.; Zhou, L.; Jiang, L.; Teng, F.; Wang, Z. Effects of high-pressure homogenization on structural and emulsifying properties of thermally soluble aggregated kidney bean (Phaseolus vulgaris L.) proteins. Food Hydrocoll. 2021, 119, 106835. [Google Scholar] [CrossRef]
- Rao, W.; Roopesh, M.S.; Pan, D.; Du, L. Enhanced Gel Properties of Duck Myofibrillar Protein by Plasma-Activated Water: Through Mild Structure Modifications. Foods 2023, 12, 877. [Google Scholar] [CrossRef]
- Zheng, Y.; Li, Z.; Zhang, C.; Zheng, B.; Tian, Y. Effects of microwave-vacuum pre-treatment with different power levels on the structural and emulsifying properties of lotus seed protein isolates. Food Chem. 2019, 311, 125932. [Google Scholar] [CrossRef] [PubMed]
- Kong, F.; Kang, S.; An, Y.; Li, W.; Han, H.; Guan, B.; Yang, M.; Zheng, Y.; Yue, X. The effect of non-covalent interactions of xylitol with whey protein and casein on structure and functionality of protein. Int. Dairy J. 2020, 111, 104841. [Google Scholar] [CrossRef]
- Wang, M.-P.; Chen, X.-W.; Guo, J.; Yang, J.; Wang, J.-M.; Yang, X.-Q. Stabilization of foam and emulsion by subcritical water-treated soy protein: Effect of aggregation state. Food Hydrocoll. 2018, 87, 619–628. [Google Scholar] [CrossRef]
- Liu, H.; Zhang, H.; Liu, Q.; Chen, Q.; Kong, B. Solubilization and stable dispersion of myofibrillar proteins in water through the destruction and inhibition of the assembly of filaments using high-intensity ultrasound. Ultrason. Sonochem. 2020, 67, 105160. [Google Scholar] [CrossRef] [PubMed]
- Taha, A.; Hu, T.; Zhang, Z.; Bakry, A.M.; Khalifa, I.; Pan, S.; Hu, H. Effect of different oils and ultrasound emulsification conditions on the physicochemical properties of emulsions stabilized by soy protein isolate. Ultrason. Sonochem. 2018, 49, 283–293. [Google Scholar] [CrossRef] [PubMed]
- Tian, R.; Feng, J.; Huang, G.; Tian, B.; Zhang, Y.; Jiang, L.; Sui, X. Ultrasound driven conformational and physicochemical changes of soy protein hydrolysates. Ultrason. Sonochem. 2020, 68, 105202. [Google Scholar] [CrossRef] [PubMed]
- Movasaghi, Z.; Rehman, S.; Rehman, I.U. Raman Spectroscopy of Biological Tissues. Appl. Spectrosc. Rev. 2007, 42, 493–541. [Google Scholar] [CrossRef]
- Xu, B.; Yuan, J.; Wang, L.; Lu, F.; Wei, B.; Azam, R.S.; Ren, X.; Zhou, C.; Ma, H.; Bhandari, B. Effect of multi-frequency power ultrasound (MFPU) treatment on enzyme hydrolysis of casein. Ultrason. Sonochem. 2019, 63, 104930. [Google Scholar] [CrossRef]
- Yang, S.; Zhang, Q.; Yang, H.; Shi, H.; Dong, A.; Wang, L.; Yu, S. Progress in infrared spectroscopy as an efficient tool for predicting protein secondary structure. Int. J. Biol. Macromol. 2022, 206, 175–187. [Google Scholar] [CrossRef]
- Yu, J.; Wang, G.; Wang, X.; Xu, Y.; Chen, S.; Wang, X.; Jiang, L. Improving the freeze-thaw stability of soy protein emulsions via combing limited hydrolysis and Maillard-induced glycation. LWT 2018, 91, 63–69. [Google Scholar] [CrossRef]
- Daniloski, D.; McCarthy, N.A.; O’Callaghan, T.F.; Vasiljevic, T. Authentication of β-casein milk phenotypes using FTIR spectroscopy. Int. Dairy J. 2022, 129, 105350. [Google Scholar] [CrossRef]
- Sadiq, U.; Gill, H.; Chandrapala, J.; Shahid, F. Influence of Spray Drying on Encapsulation Efficiencies and Structure of Casein Micelles Loaded with Anthraquinones Extracted from Aloe vera Plant. Appl. Sci. 2022, 13, 110. [Google Scholar] [CrossRef]
- Cobb, J.S.; Zai-Rose, V.; Correia, J.J.; Janorkar, A.V. FT-IR Spectroscopic Analysis of the Secondary Structures Present during the Desiccation Induced Aggregation of Elastin-Like Polypeptide on Silica. ACS Omega 2020, 5, 8403–8413. [Google Scholar] [CrossRef] [Green Version]
- Zhang, R.; Pang, X.; Lu, J.; Liu, L.; Zhang, S.; Lv, J. Effect of high intensity ultrasound pretreatment on functional and structural properties of micellar casein concentrates. Ultrason. Sonochem. 2018, 47, 10–16. [Google Scholar] [CrossRef]
- Melchior, S.; Calligaris, S.; Bisson, G.; Manzocco, L. Understanding the impact of moderate-intensity pulsed electric fields (MIPEF) on structural and functional characteristics of pea, rice and gluten concentrates. Food Bioprocess Technol. 2020, 13, 2145–2155. [Google Scholar] [CrossRef]
- Wang, N.; Zhou, X.; Wang, W.; Wang, L.; Jiang, L.; Liu, T.; Yu, D. Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex. Ultrason. Sonochem. 2021, 80, 105808. [Google Scholar] [CrossRef]
- Nickless, E.; Holroyd, S.E. Raman imaging of protein in a model cheese system. J. Spectr. Imaging 2020, 9, 1–11. [Google Scholar] [CrossRef]
- Wen, Z. Raman spectroscopy of protein pharmaceuticals. J. Pharm. Sci. 2007, 96, 2861–2878. [Google Scholar] [CrossRef]
- Kocherbitov, V.; Latynis, J.; Misiuì, A.; Barauskas, J.; Niaura, G. Hydration of Lysozyme Studied by Raman Spectroscopy. J. Phys. Chem. B 2013, 117, 4981–4992. [Google Scholar] [CrossRef]
- Xia, W.; Pan, S.; Cheng, Z.; Tian, Y.; Huang, X. High-Intensity Ultrasound Treatment on Soy Protein after Selectively Proteolyzing Glycinin Component: Physical, Structural, and Aggregation Properties. Foods 2020, 9, 839. [Google Scholar] [CrossRef]
Z-Average (nm) | PDI | ζ-Potential (mV) | Turbidity | Protein Solubility | Surface Hydrophobicity (Ho) | Temperature (°C) | |
---|---|---|---|---|---|---|---|
0 kV/cm | 266.8 ± 2.3 b | 0.52 ± 0.03 b | −26.6 ± 0.2 b | 0.137 ± 0.001 c | 84.9 ± 0.3 b | 164.9 ± 1.3 a | 20.3 ± 0.3 |
10 kV/cm | 276.2 ± 3.1 a | 0.61 ± 0.01 a | −30.1 ± 0.3 a | 0.152 ± 0.002 a | 87.1 ± 0.2 a | 166.0 ± 2.4 a | 21.1 ± 0.4 |
20 kV/cm | 258.2 ± 2.9 c | 0.56 ± 0.01 b | −29.3 ± 0.8 a | 0.141 ± 0.002 b | 86.4 ± 0.3 a | 160.6 ± 2.7 b | 22.3 ± 0.3 |
30 kV/cm | 257.5 ± 3.3 c | 0.59 ± 0.02 a,b | −29.5 ± 0.5 a | 0.143 ± 0.003 b | 86.6 ± 0.4 a | 159.4 ± 1.3 b | 24.2 ± 0.5 |
Peak Area (%) | |||||
---|---|---|---|---|---|
Side Chain | Intramolecular and Aggregated β-Sheet | Random Coil | α-Helix | β-Turn | |
0 kV/cm | 6.5 ± 1.2 a | 30.5 ± 2.1 c | 12.7 ± 2.3 c | 33.5 ± 2.4 a | 16.6 ± 2.1 c |
10 kV/cm | 7.9 ± 0.9 a | 39.7 ± 2.5 a | 10.8 ± 1.7 d | 20.5 ± 1.9 b | 20.9 ± 2.6 a |
20 kV/cm | 7.7 ± 1.3 a | 37.5 ± 1.9 b | 14.7 ± 1.6 b | 20.8 ± 1.5 b | 19.1 ± 1.8 b |
30 kV/cm | 7.4 ± 0.8 a | 37.6 ± 2.8 b | 15.8 ± 1.9 a | 20.5 ± 2.2 b | 18.5 ± 2.1 b |
Band frequency (cm−1) | 1605–1611 | 1618–1630 and 1685–1690 | 1630–1645 | 1652–1666 | 1670–1675 |
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Taha, A.; Casanova, F.; Talaikis, M.; Stankevič, V.; Žurauskienė, N.; Šimonis, P.; Pakštas, V.; Jurkūnas, M.; Gomaa, M.A.E.; Stirkė, A. Effects of Pulsed Electric Field on the Physicochemical and Structural Properties of Micellar Casein. Polymers 2023, 15, 3311. https://doi.org/10.3390/polym15153311
Taha A, Casanova F, Talaikis M, Stankevič V, Žurauskienė N, Šimonis P, Pakštas V, Jurkūnas M, Gomaa MAE, Stirkė A. Effects of Pulsed Electric Field on the Physicochemical and Structural Properties of Micellar Casein. Polymers. 2023; 15(15):3311. https://doi.org/10.3390/polym15153311
Chicago/Turabian StyleTaha, Ahmed, Federico Casanova, Martynas Talaikis, Voitech Stankevič, Nerija Žurauskienė, Povilas Šimonis, Vidas Pakštas, Marijus Jurkūnas, Mohamed A. E. Gomaa, and Arūnas Stirkė. 2023. "Effects of Pulsed Electric Field on the Physicochemical and Structural Properties of Micellar Casein" Polymers 15, no. 15: 3311. https://doi.org/10.3390/polym15153311