Extraction and modification of protein from sesame oil cake by the application of emerging technologies

• Published in: Food chemistry advances Vol. 2; p. 100326
• Main Authors: Mathews, Abin, Tangirala, A.D. Srikanth, Thirunavookarasu S, Nirmal, Kumar, Sumit, Anandharaj, Arunkumar, Rawson, Ashish
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.10.2023; Elsevier
• Subjects: Defatted sesame meal; Nonthermal technologies; Protein isolate; Sesame allergen; Techno-functional characteristics; Sesame allergen; Defatted sesame meal; Protein isolate; Nonthermal technologies; Techno-functional characteristics
• ISSN: 2772-753X; 2772-753X
• DOI: 10.1016/j.focha.2023.100326

•Valorization of sesame processing by-product.•Emerging technologies improved protein extraction yield.•Sonication retained the protein quality as well as higher extraction yield.•Fick's law of mass transfer explained the extraction kinetics of protein using emergent technologies.•Possible structural changes of allergen proteins. Present work evaluated the extraction yield and quality of protein from defatted sesame meal (DSM) using ultrasound-assisted extraction (UAE), low-temperature microwave-assisted extraction (MAE), and moderate electric field-assisted extraction (MEFAE). It was observed that the application of emerging technologies as pre-treatments significantly increased protein yield from 26.4% (without pre-treatments) to 38.9% (with UAE 450 W–20 min), 36.05% for MAE (with 500 W–20 min) and 32.75% for MEFAE (with 100 V–30 min) and improved the functional properties of Sesame protein isolate (SPI). FTIR revealed Amide I to III bands in SPI, with characteristic changes in protein secondary structure. The treated sample showed higher thermal stability evident from the denaturation temperature increase from 203.41 to 221.40 °C. The protein's microstructure in this study was transformed using various extraction techniques into a compact structure with a wrinkled surface. MAE-SPI showed maximum Invitro protein digestibility as 94.44%. The molecular weight profile revealed that the SPI samples' protein bands had molecular weights between 6.5 and 200 kDa. SDS-PAGE results revealed a change in the intensity of protein bands, and all of the main allergen protein bands were degraded.