Physico-chemical and functional properties of whey protein as affected by limited papain proteolysis and selective ultrafiltration

Physico-chemical and functional properties of whey protein as affected by limited papain... Limited proteolysis of whey protein by papain at pH 6.5 and subsequent thermal unfolding at acidic pH were studied and correlations between physico-functional (solubility, foaming, emulsifying) and physico-chemical properties were determined. The optimal degree of hydrolysis (DH) for functionality was about 3.0%, characterized by a significant reduction of aggregated whey protein present in commercial ultrafiltered whey protein concentrates. From Chromatographic and electrophoretic results it may by concluded that peptidic fragments are derived from bovine serum albumin and molecular unfolded β-lactoglobulin whereas α-lactalbumin remained unaffected. Liberated peptidic fragments were found to support foaming but not emulsiflcation as determined by a selective ultrafiltration. The beneficial effects of proteolytic and thermal modification of proteins can be maximized with each protein requiring a particular protease to develop a desirable functionality at well-defined DH. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png International Dairy Journal Elsevier

Physico-chemical and functional properties of whey protein as affected by limited papain proteolysis and selective ultrafiltration

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Publisher
Elsevier
Copyright
Copyright © 1995 Elsevier Science Ltd. All rights reserved.
ISSN
0958-6946
eISSN
1879-0143
D.O.I.
10.1016/0958-6946(94)00049-2
Publisher site
See Article on Publisher Site

Abstract

Limited proteolysis of whey protein by papain at pH 6.5 and subsequent thermal unfolding at acidic pH were studied and correlations between physico-functional (solubility, foaming, emulsifying) and physico-chemical properties were determined. The optimal degree of hydrolysis (DH) for functionality was about 3.0%, characterized by a significant reduction of aggregated whey protein present in commercial ultrafiltered whey protein concentrates. From Chromatographic and electrophoretic results it may by concluded that peptidic fragments are derived from bovine serum albumin and molecular unfolded β-lactoglobulin whereas α-lactalbumin remained unaffected. Liberated peptidic fragments were found to support foaming but not emulsiflcation as determined by a selective ultrafiltration. The beneficial effects of proteolytic and thermal modification of proteins can be maximized with each protein requiring a particular protease to develop a desirable functionality at well-defined DH.

Journal

International Dairy JournalElsevier

Published: Jan 1, 1996

References

  • Fractionation of soy protein hydrolysates using ultrafiltration membranes
    Deeslie, W.D.; Cheryan, M.
  • Effect of enzymatic hydrolysis on some functional properties of whey protein
    Ku¨hler, C.A.; Stine, C.M.
  • pH and heat treatment effects on foaming of whey protein isolate
    Phillips, L.G.; Schulman, W.; Kinsella, J.E.
  • Whey peptide fractions obtained with a two-step ultrafiltration process: production and characterization
    Turgeon, S.L.; Gauthier, S.F.
  • Emulsifying property of whey peptide fractions as a function of pH and ionic strength
    Turgeon, S.L.; Gauthier, S.F.; Paquin, P.

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