A new multistep Ca2+-Induced Cold Gelation Process for ß-Lactoglobulin

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Abstract

The objective of this study was to obtain -lactoglobulin (-lg) gels at very low protein concentrations using a new multistep Ca2+-induced cold gelation process. In the conventional cold gelation process, salt free -lg solutions were heated at neutral pH, cooled, and cross-linked by adding salts. In our new process, first, long linear -lg fibrils were formed at pH 2. Solutions of these fibrils were cooled, and subsequently, the pH was adjusted to 7 or 8. Transmission electron microscopy studies showed that the long linear fibrils formed at pH 2 were stable when the pH was adjusted to 7 or 8. In the final step, the fibrils were cross-linked using CaCl2. Using rheological measurements, the critical percolation concentration was determined. In the new multistep cold gelation process, the critical percolation concentration was an order of magnitude lower than in the conventional cold gelation method. Keywords: -lactoglobulin; cold gelation; fibrils; critical percolation concentration
Original languageEnglish
Pages (from-to)3880-3885
JournalJournal of Agricultural and Food Chemistry
Volume51
Issue number13
DOIs
Publication statusPublished - 2003

Keywords

  • whey-protein isolate
  • heat-denatured whey
  • bovine serum-albumin
  • globular-proteins
  • set gels
  • low ph
  • percolation
  • model
  • cacl2

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