4.7 Article

Influence of ohmic heating on the structural and immunoreactive properties of soybean proteins

期刊

LWT-FOOD SCIENCE AND TECHNOLOGY
卷 148, 期 -, 页码 -

出版社

ELSEVIER
DOI: 10.1016/j.lwt.2021.111710

关键词

Ohmic heating; Electrical frequency; Electric field; Electrochemical reactions; Immunoreactivity

资金

  1. Portuguese Foundation for Science and Technology (FCT) [UIDB/04469/2020, UID/QUI/50006/2020]
  2. FCT/MCTES
  3. AgriFood XXI RDI project [NORTE-01-0145-FEDER-000041, NORTE010145FEDER000052]
  4. European Regional Development Fund (FEDER) through NORTE 2020 (Northern Regional Operational Program 2014/2020)
  5. European Union (FEDER funds) [COMPETE POCI-01-0145-FEDER-031720]
  6. FCT [PTDC/BAAAGR/31720/2017, SFRH/BPD/102404/2014]
  7. FCT

向作者/读者索取更多资源

This study investigated the impact of Ohmic heating on soybean protein isolate, revealing that parameters such as electrical frequency and occurrence of electrochemical reactions can affect the structure and immunoreactivity of SPI fractions.
Ohmic heating (OH) encompasses interesting benefits towards thermal processing. Envisaging an increasing relevance of soybean protein as an alternative non-animal protein, it is important to understand how OH can contribute to the quality and immunoreactivity of soybean-derived products. This study describes, for the first time, the impact of OH when applied at different electrical frequencies (50 Hz-20 kHz) and moderate electric field intensities (up to 20 V/cm), on the leakage of metals from the electrodes and immunoreactivity aspects of soybean protein isolate (SPI). This was achieved by monitoring the occurrence of electrochemical reactions and evaluating IgG-binding capacity. OH performed at 50 Hz and 95 degrees C induced significant alterations on the intrinsic fluorescence of SPI (p <= 0.05) and the release of detectable amounts of Fe/Ni, with a subsequent reduction of 36% in the immunoreactivity of Gly m TI. The occurrence of non-thermal effects, as well as the interaction between protein and trace metals, may result in a partial blockage of protein epitopes, thus impairing specific antibody binding. These findings present novel information about the importance of OH parameters, such as electrical frequency and occurrence of electrochemical reactions, which can affect the structure and immunoreactivity of SPI fractions.

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