Peptidomic screening of bitter and nonbitter casein hydrolysate fractions for insulinogenic peptides

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  • N. M. Murray, University College Dublin
  • ,
  • D. O'Riordan, University College Dublin
  • ,
  • J. C. Jacquier, University College Dublin
  • ,
  • M. O'Sullivan, University College Dublin
  • ,
  • T. A. Holton, University College Dublin
  • ,
  • K. Wynne, University College Dublin
  • ,
  • R. C. Robinson, University of California
  • ,
  • D. Barile
  • ,
  • Søren Drud-Heydary Nielsen
  • David C. Dallas, Oregon State University
Sodium caseinate hydrolysates (NaCaH) contain biologically active peptides that can positively influence human health. However, their intense bitterness hinders their inclusion in food products. To our knowledge, no studies have investigated whether a correlation between bitterness and bioactivity exists in NaCaH, so it is not yet known what effect selective removal of bitterness has on NaCaH bioactivity. A deeper understanding of the physicochemical characteristics affecting both bitterness and bioactivity is therefore needed. The aim of this study was to use in silico analysis to elucidate the relationship between bitterness and bioactivity of the insulinogenic NaCaH. The NaCaH fractions were generated by membrane filtration and flash chromatography and were subsequently evaluated for bitterness by a sensory panel. In this present study, peptidomic and bioinformatic processing of these NaCaH fractions allowed for the identification of insulinogenic peptides as well as other literature-identified peptides in each of the fractions. The results showed that the most bitter fraction contained the highest abundance of insulinogenic peptides, whereas another bitter fraction contained the highest abundance of other literature-identified bioactive peptides exhibiting angiotensin-converting enzyme-inhibition activity. Although some bioactive peptides were identified in the least bitter fractions, the abundance of these peptides was very low. These observations show a correlation between bitter taste and bioactivity, highlighting potential complications in removing bitterness while maintaining bioactivity. However, as the most bitter fraction contained the highest abundance of insulinogenic peptides, there is potential for using a lower dose of this enriched bioactive fraction to exert health benefits. The second most bitter fraction contained a very low abundance of insulinogenic peptides and other bioactive peptides. Therefore, removal of this fraction could reduce the NaCaH product's bitterness without significantly altering overall bioactive potential.
TidsskriftJournal of Dairy Science
Sider (fra-til)2826-2837
Antal sider12
StatusUdgivet - apr. 2018
Eksternt udgivetJa


  • Bioactivity, bitterness, casein hydrolysate, insulinogenic peptide, peptidomic approach

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