1,092
Views
8
CrossRef citations to date
0
Altmetric
Original Article

Formation of high-elasticity and high-strength semitransparent ovalbumin gel induced by alkali-heat treatment

, , , &
Pages 907-923 | Received 27 Dec 2021, Accepted 21 Apr 2022, Published online: 04 May 2022

References

  • Luo, W. X.; Xue, H.; Xiong, C. H.; Li, J. K.; Tu, Y. G.; Zhao, Y. Effects of Temperature on Quality of Preserved Eggs during Storage [J]. Poultr. Sci. 2020, 99(6), 3144–3157. DOI: 10.1016/j.psj.2020.01.020.
  • Zhao, Y.; Cao, D. H.; Shao, Y. Y.; Xiong, C. H.; Li, J. K.; Tu, Y. G. Changes in Physico-chemical Properties, Microstructures, Molecular Forces and Gastric Digestive Properties of Preserved Egg White during Pickling with the Regulation of Different Metal Compounds [J]. Food Hydrocolloids. 2020, 98. DOI: 10.1016/j.foodhyd.2019.105281.
  • Zhang, X. W.; Jiang, A. M.; Chen, M. T.; Ockerman, H. W.; Chen, J. J. Effect of Different Alkali Treatments on the Chemical Composition, Physical Properties, and Microstructure of Pidan White [J]. J. Food Sci. Technol. 2013, 52(4), 2264–2271. DOI: 10.1007/s13197-013-1201-x.
  • Zhao, Y.; Chen, Z. Y.; Li, J. K.; Xu, M. S.; Shao, Y. Y.; Tu, Y. G. Changes of Microstructure Characteristics and Intermolecular Interactions of Preserved Egg White Gel during Pickling [J]. Food Chem. 2016, 203, 323–330. DOI: 10.1016/j.foodchem.2016.02.044.
  • Cai, J.; Sweeney, A. M. The Proof Is in the Pidan: Generalizing Proteins as Patchy Particles [J]. ACS Cent. Sci. 2018, 4(7), 840–853. DOI: 10.1021/acscentsci.8b00187.
  • Ganasen, P.; Benjakul, S. Physical Properties and Microstructure of Pidan Yolk as Affected by Different Divalent and Monovalent Cations [J]. LWT - Food Sci. Technol. 2010, 43(1), 77–85. DOI: 10.1016/j.lwt.2009.06.007.
  • Ganasen, P.; Benjakul, S. Chemical Composition, Physical Properties and Microstructure of Pidan White as Affected by Different Divalent and Monovalent Cations [J]. J. Food Biochem. 2011, 35(5), 1528–1537. DOI: 10.1111/j.1745-4514.2010.00475.x.
  • Zhao, Y.; Xu, M. S.; Tu, Y. G. Research Progress in Mechanisms of Preserved Egg Processing [J]. Food Sci. 2010, 31(17), 472–475.
  • Feng, T. T.; Peng, Q.; Wang, Y.; Ye, Y. Effect of Alkali Concentration in Brine on Quality of Non-heavy-metal Quickly Salted Preserved Eggs by Cascade Alkali Adjusting Method [J]. Food Ferment. Ind. 2020, 46(10), 191–196. DOI: 10.13995/j.cnki.11-1802/ts.022026.
  • Zhang, D. C.; Wang, Y.; Lei, L.; Ye, Y. Effect of Curing Agent and Recombination on Quality of Salted Preserved Eggs without Heavy Metal [J]. Sci. Technol. Food Ind. 2021, 42(6), 43–49. DOI: 10.13386/j.1002-0306.2020050325.
  • Zhao, Y.; Tu, Y. G.; Li, J. K.; Xu, M. S.; Yang, Y. X.; Nie, X. L.; Yao, Y.; Du, H. Y. Effects of Alkaline Concentration, Temperature, and Additives on the Strength of Alkaline-induced Egg White Gel [J]. Poultr. Sci. 2014, 93(10), 2628–2635. DOI: 10.3382/ps.2013-03596.
  • Xiong, W. F.; Ren, C.; Xu, X. Y.; Li, J.; Wang, L. F.; Li, B. Thermally Induced Gelation Behavior and Fractal Analysis of Ovalbumin-carboxymethylcellulose Electrostatic Complexes [J]. Food Hydrocolloids. 2019, 91, 214–223. DOI: 10.1016/j.foodhyd.2019.01.027.
  • Lassé, M.; Deb-Choudhury, S.; Haines, S.; Larsen, N.; Gerrard, J. A.; Dyer, J. M. The Impact of pH, Salt Concentration and Heat on Digestibility and Amino Acid Modification in Egg White Protein [J]. J. Food Compost. Anal. 2015, 38, 42–48. DOI: 10.1016/j.jfca.2014.08.007.
  • Van Der Plancken, I.; Van Loey, A.; Hendrickx, M. E. Effect of Heat-treatment on the Physico-chemical Properties of Egg White Proteins: A Kinetic Study [J]. J. Food Eng. 2006, 75(3), 316–326. DOI: 10.1016/j.jfoodeng.2005.04.019.
  • Van Der Plancken, I.; Van Loey, A.; Hendrickx, M. E. G. Changes in Sulfhydryl Content of Egg White Proteins Due to Heat and Pressure Treatment [J]. J. Agricutural and Food Chemistry. 2005, 53, 5726–5733. DOI: 10.1021/jf050289.
  • Chang, C. H.; Niu, F. G.; Su, Y. J.; Qiu, Y.; Gu, L. P.; Yang, Y. J. Characteristics and Emulsifying Properties of Acid and Acid-heat Induced Egg White Protein [J]. Food Hydrocolloids. 2016, 54, 342–350. DOI: 10.1016/j.foodhyd.2015.09.026.
  • Gao, X. J.; Yao, Y.; Wu, N.; Xu, M. S.; Zhao, Y.; Tu, Y. G. The Underlying Mechanism of Alkali-induced Ovalbumin Gel Transforms to Sol: Physicochemical Properties, Structure and Quantitative Protein Degradation Analysis [J]. Food Hydrocolloids. 2021, 120. DOI: 10.1016/j.foodhyd.2021.106954.
  • Zhao, Y.; Chen, Z. Y.; Li, J. K.; Xu, M. S.; Shao, Y. Y.; Tu, Y. G. Formation Mechanism of Ovalbumin Gel Induced by Alkali [J]. Food Hydrocolloids. 2016, 61, 390–398. DOI: 10.1016/j.foodhyd.2016.04.041.
  • Gao, X. J.; Yao, Y.; Wu, N.; Xu, M. S.; Zhao, Y.; Tu, Y. G. The Sol-gel-sol Transformation Behavior of Egg White Proteins Induced by Alkali [J]. Int. J. Biol. Macromol. 2020, 155, 588–597. DOI: 10.1016/j.ijbiomac.2020.03.209.
  • Huang, X. L.; Li, J. H.; Chang, C. H.; Gu, L. P.; Su, Y. J.; Yang, Y. J. Effects of NaOH/NaCl Pickling on Heat-induced Gelation Behaviour of Egg White [J]. Food Chem. 2019, 297. DOI: 10.1016/j.foodchem.2019.06.006.
  • Li, J. H.; Zhang, Y. F.; Fan, Q.; Teng, C. H.; Xie, W. Y.; Shi, Y.; Su, Y. J.; Yang, Y. J. Combination Effects of NaOH and NaCl on the Rheology and Gel Characteristics of Hen Egg White Proteins [J]. Food Chem. 2018, 250, 1–6. doi: 10.1016/j.foodchem.2018.01.031.
  • Chen, Z. Y.; Li, J. K.; Tu, Y. G.; Zhao, Y.; Luo, X. Y.; Wang, J. J.; Wang, M. L. Changes in Gel Characteristics of Egg White under Strong Alkali Treatment [J]. Food Hydrocolloids. 2015, 45, 1–8. DOI: 10.1016/j.foodhyd.2014.10.026.
  • Zhu, Y.; Vanga, S. K.; Wang, J.; Raghavan, V. Impact of Food Processing on the Structural and Allergenic Properties of Egg White [J]. Trends Food Sci. Technol. 2018, 78, 188–196. DOI: 10.1016/j.tifs.2018.06.005.
  • Ji, L.; Liu, H. P.; Cao, C. L.; Liu, P. W.; Wang, H.; Wang, H. N. Chemical and Structural Changes in Preserved White Egg during Pickled by Vacuum Technology [J]. Food Sci. Technol. Int. 2012, 19(2), 123–131. DOI: 10.1177/1082013212442186.
  • Croguennec, T.; Renault, A.; Beaufils, S.; Dubois, -J.-J.; Pezennec, S. Interfacial Properties of Heat-treated Ovalbumin [J]. J. Colloid Interface Sci. 2007, 315(2), 627–636. 10.1016/j.jcis.2007.07.041.
  • Stǎnciuc, N.; Banu, I.; Turturicǎ, M.; Aprodu, I. pH and Heat Induced Structural Changes of Chicken Ovalbumin in Relation with Antigenic Properties [J]. Int. J. Biol. Macromol. 2016, 93(Pt A), 572–581. DOI: 10.1016/j.ijbiomac.2016.09.025.
  • Deng, W. X.; Wang, Y.; Zhou, X. Y.; Liu, Z. S.; Ye, Y. Effect of Heat Induction on Physicochemical Properties of Egg White during Egg Pickling [J]. Food Sci. Technol. 2021, 46(11), 74–80. DOI: 10.13684/j.cnki.spkj.2021.11.012.
  • Luo, M. J.; Luo, C. X., and Wu, G. X. Determination of Sulfhydryl Group and Disulfide Chain of Protein in Food by Ellman’s Reagent Colorimetric Method [J]. J. Zhengzhou Grain College 1986, 1, 92–95. doi:10.16433/j.cnki.issn1673-2383.1986.01.013.
  • Deng, C.; Shao, Y. Y.; Xu, M. S.; Yao, Y.; Wu, N.; Hu, H. L.; Zhao, Y.; Tu, Y. G. Effects of Metal Ions on the Physico-chemical, Microstructural and Digestion Characteristics of Alkali-induced Egg White Gel [J]. Food Hydrocolloids. 2020, 107. DOI: 10.1016/j.foodhyd.2020.105956.
  • Wu, H.; Wang, Y.; Jiang, Q.; Jiang, X.; Feng, Q.; Shi, W. Changes in Physicochemical Properties and Myofibrillar Protein Properties in Grass Carp Salted by Brining and Injection [J]. Int. J. Food Sci. Technol. 2021, 56(11), 5674–5687. DOI: 10.1111/ijfs.15108.
  • Bao, Z. J.; Wu, J. P.; Cheng, Y.; Chi, Y. J. Effects of Lipid Peroxide on the Structure and Gel Properties of Ovalbumin [J]. Process Biochem. 2017, 57, 124–130. DOI: 10.1016/j.procbio.2017.03.009.
  • Nieuwland, M.; Bouwman, W. G.; Pouvreau, L.; Martin, A. H.; De Jongh, H. H. J. Relating Water Holding of Ovalbumin Gels to Aggregate Structure [J]. Food Hydrocolloids. 2016, 52, 87–94. DOI: 10.1016/j.foodhyd.2015.06.018.
  • Wu, M. G.; Cao, Y.; Lei, S. M.; Liu, Y.; Wang, J. H.; Hu, J.; Li, Z. K.; Liu, R.; Ge, Q. F.; Yu, H. Protein Structure and Sulfhydryl Group Changes Affected by Protein Gel Properties: Process of Thermal-induced Gel Formation of Myofibrillar Protein [J]. Int. J. Food Prop. 2019, 22(1), 1834–1847. DOI: 10.1080/10942912.2019.1656231.
  • Zou, W. J.; Mourad, F. K.; Zhang, X. Y.; Ahn, D. U.; Cai, Z. X.; Jin, Y. G. Phase Separation Behavior and Characterization of Ovalbumin and Propylene Glycol Alginate Complex Coacervates [J]. Food Hydrocolloids. 2020, 108. DOI: 10.1016/j.foodhyd.2020.105978.
  • Xue, H.; Tu, Y. G.; Xu, M.; Liao, M. F.; Luo, W. X.; Guo, W. B.; Zhang, G. W.; Zhao, Y. Changes in Physicochemical Properties, Gel Structure and in Vitro Digestion of Marinated Egg White Gel during Braising [J]. Food Chem. 2020, 330. DOI: 10.1016/j.foodchem.2020.127321.
  • Mine, Y. Recent Advances in the Understanding of Egg White Protein Functionality [J]. Trends Food Sci. Technol. 1995, 6(7), 225–232. DOI: 10.1016/S0924-2244(00)89083-4.
  • Guo, W. B.; Zhao, Y.; Yao, Y.; Wu, N.; Xu, M. S.; Du, H. Y.; Tu, Y. G. Relationship between Protein Structure Changes and in Vitro Digestion of Preserved Egg White during Pickling [J]. Int. J. Biol. Macromol. 2019, 138, 116–124. DOI: 10.1016/j.ijbiomac.2019.07.057.
  • Chen, K.; Chen, X.; Liang, L.; Xu, X. L. Gallic Acid-aided Cross-linking of Myofibrillar Protein Fabricated Soluble Aggregates for Enhanced Thermal Stability and a Tunable Colloidal State [J]. J. Agric. Food Chem. 2020, 68(41), 11535–11544. DOI: 10.1021/acs.jafc.0c02059.
  • Gharbi, N.; Labbafi, M. Effect of Processing on Aggregation Mechanism of Egg White Proteins [J]. Food Chem. 2018, 252(252), 126–133. DOI: 10.1016/j.foodchem.2018.01.088.
  • Kang, Z. L.; Wang, P.; Xu, X. L.; Zhu, C. Z.; Li, K.; Zhou, G. H. Effect of Beating Processing, as a Means of Reducing Salt Content in Frankfurters: A Physico-chemical and Raman Spectroscopic Study [J]. Meat Sci. 2014, 98(2), 171–177. DOI: 10.1016/j.meatsci.2014.05.025.
  • Pérez-Mateos, M.; Lourenco, H.; Montero, P. Borderías, A. J. Rheological and Biochemical Characteristics of High-Pressure- and Heat-Induced Gels from Blue Whiting (Micromesistius Poutassou) Muscle Proteins. J. Agricutural and Food Chemistry. 1997, 451, 44–49. DOI:10.1021/jf960185m.
  • Khemakhem, M.; Attia, H.; Ayadi, M. A. The Effect of pH, Sucrose, Salt and Hydrocolloid Gums on the Gelling Properties and Water Holding Capacity of Egg White Gel [J]. Food Hydrocolloids. 2019, 87, 11–19. DOI: 10.1016/j.foodhyd.2018.07.041.
  • Urbonaite, V.; De Jongh, H. H. J.; Van Der, L. E.; Pouvreau, L. Permeability of Gels Is Set by the Impulse Applied on the Gel [J]. Food Hydrocolloids. 2015, 50, 7–15. DOI: 10.1016/j.foodhyd.2015.03.024.
  • Urbonaite, V.; De Jongh, H. H. J.; Van Der, L. E.; Pouvreau, L. Water Holding of Soy Protein Gels Is Set by Coarseness, Modulated by Calcium Binding, Rather than Gel Stiffness [J]. Food Hydrocolloids. 2015, 46, 103–111. DOI: 10.1016/j.foodhyd.2014.12.010.
  • Ai, M. M.; Zhou, Q.; Xiao, N.; Guo, S. G.; Cao, Y. Y.; Fan, H.; Ling, Z. T.; Zhou, L. D.; Li, S. C.; Long, J. L., et al. Enhancement of Gel Characteristics of NaOH-induced Duck Egg White Gel by Adding Ca(OH)2 With/without Heating [J]. Food Hydrocolloids. 2020, 103. DOI: 10.1016/j.foodhyd.2020.105654.
  • Fernández-López, J.; Martínez, A.; Fernández-Ginés, J. M.; Sayas-Barberá, E.; Sendra, E.; Pérez-Alvarez, J. A. Gelling and Color Properties of Ostrich (Struthio Camelus) Egg White [J]. J. Food Qual. 2006, 29(2), 171–183. DOI: 10.1111/j.1745-4557.2006.00065.x.
  • Herrero, A. M. Raman Spectroscopy for Monitoring Protein Structure in Muscle Food Systems [J]. Food Sci. Nutr. 2008, 48(6), 512–523. DOI: 10.1080/10408390701537385.
  • Ngarize, S.; Herman, H.; Adams, A.; Howell, N. Comparison of Changes in the Secondary Structure of Unheated, Heated, and High-pressure-treated Beta-lactoglobulin and Ovalbumin Proteins Using Fourier Transform Raman Spectroscopy and Self-deconvolution [J]. J. Agricultural and Food Chemistry. 2004, 5221, 6470–6477. DOI:10.1021/jf030649y.
  • Xu, L. L.; Zhao, Y.; Xu, M. S.; Yao, Y.; Wu, N.; Du, H. Y.; Tu, Y. G. Changes in Physico-chemical Properties, Microstructure, Protein Structures and Intermolecular Force of Egg Yolk, Plasma and Granule Gels during Salting [J]. Food Chem. 2019, 275, 600–609. DOI: 10.1016/j.foodchem.2018.09.078.
  • Li, K.; Zhao, Y. Y.; Kang, Z. L.; Wang, H. H.; Ma, H. J.; Xu, X. L. Effect of NaCl on Processing Characteristics and Protein Secondary Structures in Pork Meat Batters [J]. Food Sci. 2017, 38(15). DOI: 10.7506/spkx1002-6630-201715013.
  • Yang, Y.; Zhao, Y.; Xu, M.; Yao, Y.; Wu, N.; Du, H.; Tu, Y. Effects of Strong Alkali Treatment on the Physicochemical Properties, Microstructure, Protein Structures, and Intermolecular Forces in Egg Yolks, Plasma, and Granules [J]. Food Chem. 2020, 311, 125998. DOI: 10.1016/j.foodchem.2019.125998.
  • Kaewmanee, T.; Benjakul, S.; Visessanguan, W. Effects of Salting Processes and Time on the Chemical Composition, Textural Properties, and Microstructure of Cooked Duck Egg [J]. J. Food Sci. 2011, 76(2), S139–S147. DOI: 10.1111/j.1750-3841.2010.01975.x.
  • Zhao, Y.; Tu, Y. G.; Xu, M. S.; Li, J. K.; Du, H. Y. Physicochemical and Nutritional Characteristics of Preserved Duck Egg White [J]. Poultr. Sci. 2014, 93(12), 3130–3137. DOI: 10.3382/ps.2013-03823.