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Effect of pulsed electric field on the secondary structure and thermal properties of soy protein isolate

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Abstract

Changes of structure and thermal stability of soy protein isolate after pulsed electric field treatment were analyzed by Fourier transform infrared spectroscopy and differential scanning calorimetry (DSC). When the applied pulsed electric field (PEF) treatment intensity was over 35 kV/cm, the amino acid side chain, anti-parallel β-sheets, β-turn as well as β-sheets in soy protein isolate (SPI) secondary structure were significantly changed, which suggested that PEF treatment might be a new processing method for SPI; the dipole moments of some bonds, such as C=O, C–O, and C–O–C were partially polarized, accompanying with complete denaturation of β-conglycinin and glycinin obtained from DSC. Furthermore, self-reassembly from β-turn to α-helix in SPI structure abruptly happened under intense PEF treatment condition, which suggested that the PEF treatment had induced change of the orientation of α-helix dipole moment to stabilize α-helix. This observation implies that PEF treatment technique may be a novel method for preparation of protein nanotube.

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Acknowledgments

This study was supported by the Fundamental Research Funds for the Central Universities, SCUT(2009ZZ0057), the Chinese National “863” project (2011AA100801) as well as the Chinese National Natural Science Fund (2107608).

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Authors and Affiliations

  1. College of Food Sciences and Light Industry, South China University of Technology, Guangzhou, 510640, People’s Republic of China

    Yan Yan Liu, Xin An Zeng & Shu Juan Yu

  2. Department of Plant Biology, Carnegie Institution for Science, Stanford, CA, 94305, USA

    Zhiping Deng

  3. Graduate School of Life and Environmental Sciences, Osaka Prefecture University, 1-58, Rinku Ourai-kita, Izumisano, Osaka, 598-8531, Japan

    Shinji Yamasaki

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  1. Yan Yan Liu
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Correspondence to Xin An Zeng.

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Liu, Y.Y., Zeng, X.A., Deng, Z. et al. Effect of pulsed electric field on the secondary structure and thermal properties of soy protein isolate. Eur Food Res Technol 233, 841–850 (2011). https://doi.org/10.1007/s00217-011-1580-z

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  • DOI: https://doi.org/10.1007/s00217-011-1580-z

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