Abstract
Proteins represent one of the major food components that contribute to a wide range of biophysical functions and dictate the nutritional, sensorial, and shelf-life of food products. Different non-thermal processing technologies (e.g., irradiation, ultrasound, cold plasma, pulsed electric field, and high-pressure treatments) can affect the structure of proteins, and thus their solubility as well as their functional properties. The exposure of hydrophobic groups, unfolding followed by aggregation at high non-thermal treatment intensities, and the formation of new bonds have been reported to promote the modification of structural and functional properties of proteins. Several studies reported the reduction of allergenicity of some proteins after the application of non-thermal treatments. The composition and concentration of free amino acids could be changed after non-thermal processing, depending on the processing time and intensity. The present review discusses the effects of different non-thermal treatments on protein properties in detail, and highlights the opportunities and disadvantages of these technologies in relation to protein functionality.
| Original language | English (US) |
|---|---|
| Article number | 262 |
| Journal | Foods |
| Volume | 8 |
| Issue number | 7 |
| DOIs | |
| State | Published - Jul 1 2019 |
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Keywords
- Amino acids
- Cold plasma
- High-pressure processing
- Irradiation
- Proteins
- Pulsed electric fields
- Ultrasound
PubMed: MeSH publication types
- Journal Article
- Review
Cite this
Bridging the knowledge gap for the impact of non-thermal processing on proteins and amino acids. / Esteghlal, Sara; Gahruie, Hadi Hashemi; Niakousari, Mehrdad; Barba, Francisco J.; Bekhit, Alaa El Din; Mallikarjunan, Kumar; Roohinejad, Shahin.
In: Foods, Vol. 8, No. 7, 262, 01.07.2019.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - Bridging the knowledge gap for the impact of non-thermal processing on proteins and amino acids
AU - Esteghlal, Sara
AU - Gahruie, Hadi Hashemi
AU - Niakousari, Mehrdad
AU - Barba, Francisco J.
AU - Bekhit, Alaa El Din
AU - Mallikarjunan, Kumar
AU - Roohinejad, Shahin
PY - 2019/7/1
Y1 - 2019/7/1
N2 - Proteins represent one of the major food components that contribute to a wide range of biophysical functions and dictate the nutritional, sensorial, and shelf-life of food products. Different non-thermal processing technologies (e.g., irradiation, ultrasound, cold plasma, pulsed electric field, and high-pressure treatments) can affect the structure of proteins, and thus their solubility as well as their functional properties. The exposure of hydrophobic groups, unfolding followed by aggregation at high non-thermal treatment intensities, and the formation of new bonds have been reported to promote the modification of structural and functional properties of proteins. Several studies reported the reduction of allergenicity of some proteins after the application of non-thermal treatments. The composition and concentration of free amino acids could be changed after non-thermal processing, depending on the processing time and intensity. The present review discusses the effects of different non-thermal treatments on protein properties in detail, and highlights the opportunities and disadvantages of these technologies in relation to protein functionality.
AB - Proteins represent one of the major food components that contribute to a wide range of biophysical functions and dictate the nutritional, sensorial, and shelf-life of food products. Different non-thermal processing technologies (e.g., irradiation, ultrasound, cold plasma, pulsed electric field, and high-pressure treatments) can affect the structure of proteins, and thus their solubility as well as their functional properties. The exposure of hydrophobic groups, unfolding followed by aggregation at high non-thermal treatment intensities, and the formation of new bonds have been reported to promote the modification of structural and functional properties of proteins. Several studies reported the reduction of allergenicity of some proteins after the application of non-thermal treatments. The composition and concentration of free amino acids could be changed after non-thermal processing, depending on the processing time and intensity. The present review discusses the effects of different non-thermal treatments on protein properties in detail, and highlights the opportunities and disadvantages of these technologies in relation to protein functionality.
KW - Amino acids
KW - Cold plasma
KW - High-pressure processing
KW - Irradiation
KW - Proteins
KW - Pulsed electric fields
KW - Ultrasound
UR - http://www.scopus.com/inward/record.url?scp=85069223222&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85069223222&partnerID=8YFLogxK
U2 - 10.3390/foods8070262
DO - 10.3390/foods8070262
M3 - Review article
C2 - 31319521
AN - SCOPUS:85069223222
VL - 8
JO - Foods
JF - Foods
SN - 2304-8158
IS - 7
M1 - 262
ER -