Bridging the knowledge gap for the impact of non-thermal processing on proteins and amino acids

Sara Esteghlal, Hadi Hashemi Gahruie, Mehrdad Niakousari, Francisco J. Barba, Alaa El Din Bekhit, Kumar Mallikarjunan, Shahin Roohinejad

Research output: Contribution to journalReview articlepeer-review

8 Scopus citations


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 languageEnglish (US)
Article number262
Issue number7
StatePublished - Jul 2019

Bibliographical note

Publisher Copyright:
© 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (


  • Amino acids
  • Cold plasma
  • High-pressure processing
  • Irradiation
  • Proteins
  • Pulsed electric fields
  • Ultrasound


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