Enzymatic hydrolysis as a means of expanding the cold gelation conditions of soy proteins

B.J.H. Kuipers, G.A. van Koningsveld, A.C. Alting, F. Driehuis, H. Gruppen, A.G.J. Voragen

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45 Citations (Scopus)


Acid-induced cold gelation of soy protein hydrolysates was studied. Hydrolysates with degrees of hydrolysis (DH) of up to 10% were prepared by using subtilisin Carlsberg. The enzyme was inhibited to uncouple the hydrolysis from the subsequent gelation; the latter was induced by the addition of glucono--lactone. Visual observations, confocal scanning laser microscopy images, and the elasticity modulus showed that hydrolysates gelled at higher pH values with increasing DH. The nonhydrolyzed soy protein isolate gelled at pH ~6.0, whereas a DH = 5% hydrolysate gelled at pH ~7.6. Gels made from hydrolysates had a softer texture when manually disrupted and showed syneresis below a pH of 5-5.5. Monitoring of gelation by measuring the development of the storage modulus could be replaced by measuring the pH onset of aggregate formation (pHAggr-onset) using turbidity measurements. The rate of acidification was observed to also influence this pHAggr-onset. Changes in ionic strength (0.03, 0.2, and 0.5 M) had only a minor influence on the pHAggr-onset, indicating that the aggregation is not simply a balance between repulsive electrostatic and attractive hydrophobic interactions, but is much more complex.
Original languageEnglish
Pages (from-to)1031-1038
JournalJournal of Agricultural and Food Chemistry
Issue number4
Publication statusPublished - 2005


  • whey proteins
  • rheological properties
  • beta-lactoglobulin
  • globular-proteins
  • food proteins
  • heat
  • protease
  • gels
  • aggregation
  • isolate

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