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Differential scanning calorimetry of lupin and soy proteins

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Abstract

Differential scanning calorimetry (DSC) was used to study the 7S and 11S globulin fractions extracted from lupin seed (Lupinus luteus) flour. In agreement with previous work on other lupin species, the isolate showed three denaturation peaks compared to the two observed with soy. By comparison with the isolated globulin fractions, the denaturation peaks at the two higher temperatures in the lupin isolate were assigned to the 11S and 7S globulins. The denaturation temperature of the lupin 7S globulin was about 10 K higher than that for the corresponding soy globulin, whereas the values for the 11S globulin were similar. All globulins displayed increasing thermal stability with decreasing moisture contents. Possible reasons for the differences in behaviour of soy and lupin protein isolates are discussed.

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Authors and Affiliations

  1. SACTA, Instituto Superior de Agronomia, Universidade Técnica de Lisboa, Tapada da Ajuda, P-1399, Lisboa Codex, Portugal

    Isabel M. N. Sousa & M. Luisa Beirão da Costa

  2. Department, of Applied Biochemistry and Food Science, University of Nottingham, Sutton Bonington Campus, 12 5RD, Loughborough, LE, UK

    John R. Mitchell & Sandra E. Hill

  3. Department of Food Science, University of Reading, Whiteknights, Reading, Berks, UK

    Dave A. Ledward

Authors
  1. Isabel M. N. Sousa
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  2. John R. Mitchell
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  3. Dave A. Ledward
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  4. Sandra E. Hill
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  5. M. Luisa Beirão da Costa
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Sousa, I.M.N., Mitchell, J.R., Ledward, D.A. et al. Differential scanning calorimetry of lupin and soy proteins. Z Lebensm Unters Forch 201, 566–569 (1995). https://doi.org/10.1007/BF01201587

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  • DOI: https://doi.org/10.1007/BF01201587

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