Hostname: page-component-586b7cd67f-l7hp2 Total loading time: 0 Render date: 2024-11-23T10:29:32.322Z Has data issue: false hasContentIssue false

Separation of bovine κ-casein glycomacropeptide from sweet whey protein products with undetectable level of phenylalanine by protein precipitation followed by anion exchange chromatography

Published online by Cambridge University Press:  22 February 2018

Takuo Nakano*
Affiliation:
Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta, T6G 2P5Canada
Lech Ozimek
Affiliation:
Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta, T6G 2P5Canada
Mirko Betti
Affiliation:
Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta, T6G 2P5Canada
*
*For correspondence; e-mail: [email protected]

Abstract

Bovine κ-casein glycomacropeptide (GMP) found in sweet whey is a 64 amino acid residue glycopeptide, which does not contain phenylalanine or other aromatic amino acids. There is, however, little information available concerning isolation of phenylalanine free GMP from sweet whey. In the study reported in this Research Communication, GMP was purified from three samples of sweet whey protein products (SWPP) by a procedure involving: (1) precipitation of protein by heat treatment; (2) precipitation of protein by pH shift to 4·6; and (3) diethylaminoethyl (DEAE)-Sephacel anion exchange chromatography of soluble portion of each sample obtained after removal of protein precipitates. The total protein precipitated with both heat treatment and pH shift accounted for average 61% of dry weight of SWPP. The GMP fraction obtained by DEAE-Sephacel chromatography accounted for average 7·5% of dry weight of SWPP. Amino acid analysis showed that there was no detectable level of phenylalanine in GMP fractions from all samples examined. The present method may help develop large scale methods of production of GMP.

Type
Research Article
Copyright
Copyright © Hannah Dairy Research Foundation 2018 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Abd El-Salam, MH 2006 Separation of casein glycomacropeptide from whey: methods of potential industrial application. International Journal of Dairy Technology 1 9399 Google Scholar
AOAC 1998 Official Methods of Analysis of AOAC International, 16th edition. Gaithersburg, MD: Association of Official Analytical Chemists Google Scholar
Brody, EP 2000 Biological activities of bovine glycomacropeptide. British Journal of Nutrition 84 S39S46 Google Scholar
Eigel, WN, Butler, JE, Ernstrom, CA, Farrel, HM Jr, Harwalker, VR, Jeness, R & Whitney, RMcL 1984 Nomenclature of proteins of cow's milk. Fifth revision. Journal of Dairy Science 67 15991631 Google Scholar
Léonil, J & Mollè, D 1991 A method for determination of macropeptide by cation-exchange fast protein liquid chromatography and its use for following the action of chymosin in milk. Journal of Dairy Research 58 321328 Google Scholar
Nakano, T, Ikawa, N & Ozimek, L 2007 Detection of sialylated phosphorylated κ-casein glycomacropeptide electrophoresed on polyacrylamide gels and cellulose acetate strips by the thiobarbituric acid and malachite green dye reactions. Journal of Agricultural and Food Chemistry 55 27142726 Google Scholar
Nakano, T & Ozimek, L 1999 Purification of glycomacropeptide from non-dialyzable fraction of sweet whey by anion-exchange chromatography. Biotechnology Techniques 13 739742 CrossRefGoogle Scholar
Nakano, T & Ozimek, L 2015 Selective removal of phenylalanine impurities from commercial κ- casein glycomacropeptide by anion exchange chromatography. Journal of Food Processing & Technology 7 537. doi: 10.4172/2157-7110. 1000537 Google Scholar
Supplementary material: PDF

Nakano et al. supplementary material

Tables S1-S4 and Figure S1

Download Nakano et al. supplementary material(PDF)
PDF 268.8 KB