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Colloidal stability of oil-in-water emulsions prepared from hen egg white submitted to dry and/or wet heating to induce amyloid-like fibril formation

Arne Huyst (UGent) , Lomme J. Deleu, Trui Luyckx (UGent) , Dieter Buyst (UGent) , John Van Camp (UGent) , Jan A. Delcour and Paul Van der Meeren (UGent)
(2022) FOOD HYDROCOLLOIDS. 125.
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Abstract
Hen egg white (HEW) proteins are components of some foods and improvement of their techno-functional properties has been widely studied. During food processing, they are commonly subjected to heating. Here, both the impact of dry, wet, and combined dry and wet heat treatment was investigated. Heating (1 h at 80 degrees C) dried HEW (still containing 12% water) resulted in formation of glycated Maillard compounds such as proteinglucose conjugates, but only in limited amyloid-like fibril (ALF) formation. Wet heating (0.5 hat 80 degrees C, in excess water) clearly resulted in increased relative Thioflavin T (ThT) fluorescence, indicating the formation of ALFs. When dry heating (0.5 h at 80 degrees C) was followed by wet heating (24 h at 80 degrees C), the slightly lower relative ThT fluorescence than obtained when wet heating HEW suggested that ALF formation was limited due to protein glycation. When control (i.e. unheated) HEW dispersions and dispersions containing different heated HEW samples were used as continuous phase for oil-in-water emulsions, control HEW resulted in a multimodal particle size distribution and high creaming rate. In contrast, emulsions stabilized by dry and wet heated HEW showed an overall reduced volume-weighted average droplet diameter (D43) and increased creaming stability. HEW subjected to 4 h dry heat treatment at 80 degrees C and 24 h wet heat treatment at 80 degrees C resulted in emulsions with a monomodal particle size distribution with the smallest D43 (0.47 +/- 0.01 mu m), as well as the lowest creaming rate (68.4 +/- 9.77 mm/day). Comparison of the relative ThT fluorescence, D43 and creaming rate by principal component analysis revealed that mainly the emulsions with dispersions having high relative ThT fluorescence had lower average particle sizes and consequently a higher creaming stability. Thus, formation of ALFs by wet heating of HEW seems to be the better heat treatment for improving their techno-functional properties.
Keywords
General Chemical Engineering, General Chemistry, Food Science, Amyloid-like fibril, Conjugation, Dry and wet heat, Hen egg white, Oil-in-water emulsion, WHEY-PROTEIN ISOLATE, FUNCTIONAL-PROPERTIES, MAILLARD REACTION, PRODUCTS, STABILIZATION, LYSOZYME, GLUCOSE

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MLA
Huyst, Arne, et al. “Colloidal Stability of Oil-in-Water Emulsions Prepared from Hen Egg White Submitted to Dry and/or Wet Heating to Induce Amyloid-like Fibril Formation.” FOOD HYDROCOLLOIDS, vol. 125, 2022, doi:10.1016/j.foodhyd.2021.107450.
APA
Huyst, A., Deleu, L. J., Luyckx, T., Buyst, D., Van Camp, J., Delcour, J. A., & Van der Meeren, P. (2022). Colloidal stability of oil-in-water emulsions prepared from hen egg white submitted to dry and/or wet heating to induce amyloid-like fibril formation. FOOD HYDROCOLLOIDS, 125. https://doi.org/10.1016/j.foodhyd.2021.107450
Chicago author-date
Huyst, Arne, Lomme J. Deleu, Trui Luyckx, Dieter Buyst, John Van Camp, Jan A. Delcour, and Paul Van der Meeren. 2022. “Colloidal Stability of Oil-in-Water Emulsions Prepared from Hen Egg White Submitted to Dry and/or Wet Heating to Induce Amyloid-like Fibril Formation.” FOOD HYDROCOLLOIDS 125. https://doi.org/10.1016/j.foodhyd.2021.107450.
Chicago author-date (all authors)
Huyst, Arne, Lomme J. Deleu, Trui Luyckx, Dieter Buyst, John Van Camp, Jan A. Delcour, and Paul Van der Meeren. 2022. “Colloidal Stability of Oil-in-Water Emulsions Prepared from Hen Egg White Submitted to Dry and/or Wet Heating to Induce Amyloid-like Fibril Formation.” FOOD HYDROCOLLOIDS 125. doi:10.1016/j.foodhyd.2021.107450.
Vancouver
1.
Huyst A, Deleu LJ, Luyckx T, Buyst D, Van Camp J, Delcour JA, et al. Colloidal stability of oil-in-water emulsions prepared from hen egg white submitted to dry and/or wet heating to induce amyloid-like fibril formation. FOOD HYDROCOLLOIDS. 2022;125.
IEEE
[1]
A. Huyst et al., “Colloidal stability of oil-in-water emulsions prepared from hen egg white submitted to dry and/or wet heating to induce amyloid-like fibril formation,” FOOD HYDROCOLLOIDS, vol. 125, 2022.
@article{8736230,
  abstract     = {{Hen egg white (HEW) proteins are components of some foods and improvement of their techno-functional properties has been widely studied. During food processing, they are commonly subjected to heating. Here, both the impact of dry, wet, and combined dry and wet heat treatment was investigated. Heating (1 h at 80 degrees C) dried HEW (still containing 12% water) resulted in formation of glycated Maillard compounds such as proteinglucose conjugates, but only in limited amyloid-like fibril (ALF) formation. Wet heating (0.5 hat 80 degrees C, in excess water) clearly resulted in increased relative Thioflavin T (ThT) fluorescence, indicating the formation of ALFs. When dry heating (0.5 h at 80 degrees C) was followed by wet heating (24 h at 80 degrees C), the slightly lower relative ThT fluorescence than obtained when wet heating HEW suggested that ALF formation was limited due to protein glycation. When control (i.e. unheated) HEW dispersions and dispersions containing different heated HEW samples were used as continuous phase for oil-in-water emulsions, control HEW resulted in a multimodal particle size distribution and high creaming rate. In contrast, emulsions stabilized by dry and wet heated HEW showed an overall reduced volume-weighted average droplet diameter (D43) and increased creaming stability. HEW subjected to 4 h dry heat treatment at 80 degrees C and 24 h wet heat treatment at 80 degrees C resulted in emulsions with a monomodal particle size distribution with the smallest D43 (0.47 +/- 0.01 mu m), as well as the lowest creaming rate (68.4 +/- 9.77 mm/day). Comparison of the relative ThT fluorescence, D43 and creaming rate by principal component analysis revealed that mainly the emulsions with dispersions having high relative ThT fluorescence had lower average particle sizes and consequently a higher creaming stability. Thus, formation of ALFs by wet heating of HEW seems to be the better heat treatment for improving their techno-functional properties.}},
  articleno    = {{107450}},
  author       = {{Huyst, Arne and Deleu, Lomme J. and Luyckx, Trui and Buyst, Dieter and Van Camp, John and Delcour, Jan A. and Van der Meeren, Paul}},
  issn         = {{0268-005X}},
  journal      = {{FOOD HYDROCOLLOIDS}},
  keywords     = {{General Chemical Engineering,General Chemistry,Food Science,Amyloid-like fibril,Conjugation,Dry and wet heat,Hen egg white,Oil-in-water emulsion,WHEY-PROTEIN ISOLATE,FUNCTIONAL-PROPERTIES,MAILLARD REACTION,PRODUCTS,STABILIZATION,LYSOZYME,GLUCOSE}},
  language     = {{eng}},
  pages        = {{11}},
  title        = {{Colloidal stability of oil-in-water emulsions prepared from hen egg white submitted to dry and/or wet heating to induce amyloid-like fibril formation}},
  url          = {{http://dx.doi.org/10.1016/j.foodhyd.2021.107450}},
  volume       = {{125}},
  year         = {{2022}},
}
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