Use of macroporous adsorption resin for simultaneous desalting and debittering of whey protein hydrolysates

  1. Seronei C. Cheison1,2,
  2. Zhang Wang1,*,
  3. Shi-Ying Xu1

Article first published online: 27 JUL 2007

DOI: 10.1111/j.1365-2621.2006.01461.x

Issue

International Journal of Food Science & Technology

International Journal of Food Science & Technology

Volume 42, Issue 10, pages 1228–1239, October 2007

Additional Information

How to Cite

Cheison, S. C., Wang, Z. and Xu, S.-Y. (2007), Use of macroporous adsorption resin for simultaneous desalting and debittering of whey protein hydrolysates. International Journal of Food Science & Technology, 42: 1228–1239. doi: 10.1111/j.1365-2621.2006.01461.x

Author Information

  1. 1

     Southern Yangtze University, School of Food Science, Key Laboratory of Food Science and Safety, Ministry of Education, Box No. 98, No. 170 Hui He Road, Wuxi 214036, China

  2. 2

     School of Public Health and Community Development, Maseno University, P.O. Box 333, Maseno 40105, Kenya

* *Fax: 86 510 85884496; e-mail: zw@sytu.edu.cn

Publication History

  1. Issue published online: 30 JUL 2007
  2. Article first published online: 27 JUL 2007
  3. (Received 31 January 2006; Accepted in revised form 24 August 2006)

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Keywords:

  • Angiotensin-I converting enzyme inhibition;
  • bioactive peptides;
  • debitter;
  • desalt;
  • hydrophobicity;
  • macroporous adsorption resin;
  • whey protein hydrolysate

Summary

Whey protein isolate (WPI) was hydrolysed to whey protein hydrolysates (WPH) of degree of hydrolysis equal to 15% using Protease N ‘Amano’ G (IUB 3.4.24.28) in a batch reactor at 55 °C and pH 7.0 according to the pH-stat procedure. Ash was removed by adsorbing WPH onto macroporous adsorption resins (MAR). Following rinsing with deionised water, desorption was achieved by washing with 20%, 40% and 75% alcohol (v v−1) to obtain the three fractions HS20, HS40 and HS75. Ash reduced from 15.71% (WPH) to 4.38% (HS20), 2.02% (HS40) and 2.38% (HS75). Similarly, the protein content was enriched from a low of 64.89% (WPH) to 94.74% (HS20), 95.32% (HS40) and 92.00% (HS75). The fractions were analysed for surface hydrophobicity (SHo), angiotensin-I converting enzyme (ACE) inhibition, emulsifying activity index, total amino acids composition and molecular weight distribution. Fraction HS75 was objectionably bitter, showed superior ACE inhibition (lowest IC50), had the highest content of hydrophobic and essential amino acids and contained about 71% of <600 Da with no fractions exceeding 4142 Da. Desorption with alcohol weakened the hydrophobic interaction forces between the peptides and resins and hence eluted the peptides, with the bitter HS75 being extracted.

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