Influence of non-thermal microwave radiation on emulsifying properties of sunflower protein


GÜLTEKİN SUBAŞI B., ELİKOĞLU S., Altay I., Jafarpour A., Casanova F., Mohammadifar M. A. , ...More

FOOD CHEMISTRY, vol.372, 2022 (Peer-Reviewed Journal) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 372
  • Publication Date: 2022
  • Doi Number: 10.1016/j.foodchem.2021.131275
  • Journal Name: FOOD CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded, Scopus, Academic Search Premier, PASCAL, Aerospace Database, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Chimica, Communication Abstracts, Compendex, EMBASE, Food Science & Technology Abstracts, MEDLINE, Metadex, Veterinary Science Database, Civil Engineering Abstracts
  • Keywords: Non-thermal microwave, Sunflower protein, Emulsifying properties, Interfacial tension, Dilatational rheology, FOOD-PROCESSING TECHNOLOGIES, GAMMA-IRRADIATION, HOMOGENIZATION, STABILITY, ISOLATE, PLANT

Abstract

Sunflower protein isolate obtained from industrially de-oiled press cake was treated with non-thermal microwave, aiming to investigate how structure and emulsifying properties were affected. Our results indicated that the content of polar amino acids was decreased and solubility and surface hydrophobicity were altered upon exposure to non-thermal microwave. Higher solubility and surface hydrophobicity of the samples treated with defrost mode and also 350 W were accompanied by a smaller size and lower uniformity of the oil droplets compared to the control and other samples. Non-thermal microwave treatment improved the emulsion stability by 1.43 times and defrost mode treated sample had the lowest stability index after 120 min. Interfacial dilatational rheology measurements revealed that 70 and 350 W treated samples created higher elastic, less stretchable solid-like layer at the O/W interface in comparison with defrost mode treated and control samples. Consequently, non-thermal microwave treatment could be considered as a promising simple, fast, and "green" protein modification technique.