Hostname: page-component-cd9895bd7-7cvxr Total loading time: 0 Render date: 2024-12-26T07:05:07.939Z Has data issue: false hasContentIssue false

Application of the plastein reaction to caseins and to skim-milk powder: II. Chemical and physical properties of the plasteins and the mechanism of plastein formation

Published online by Cambridge University Press:  01 June 2009

Gonca Sukan
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading RG2 9 AT, UK
Anthony T. Andrews
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading RG2 9 AT, UK

Summary

Chemical and physical properties of plasteins derived from caseins and skim-milk powder have been investigated. Plasteins were very similar in properties regardless of starting material or of the proteinase used in their production. Plastein formed from Na caseinate hydrolysate at pH 5 was stable over the pH range 1·5–9·0 and had the properties of a thixotropic gel. More extreme pH values caused dissolution as did various chaotropic reagents. 8 M-urea disrupted plastein structure almost entirely, as did various organic acids at concentrations of 50% (v/v) and strongly ionic detergents. Non-ionic or weakly cationic detergents and 6 M-guanidine hydrochloride were less effective. Treatment with strong salt solutions, Ca2+ and EDTA had no effect. Gel filtration experiments demonstrated that plasteins were completely disrupted under dissociating conditions and peptide mapping confirmed that all the peptides originally present in the hydrolysate were also present in plastein. Amino group contents were unchanged on plastein formation. These experiments together with gel electrophoresis studies clearly showed that only hydrophobic and ionic bonding mechanisms were involved in plastein formation and no detectable peptide bond formation or transpeptidation occurred. In accordance with this, amino acid analysis suggested that hydrophobic peptides were preferentially incorporated. Implications for use of plasteins in food products are discussed.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1982

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

REFERENCES

Anderson, M. & Andrews, A. T. 1977 Progressive changes in individual milk protein concentrations associated with high somatic cell counts. Journal of Dairy Research 44 223235CrossRefGoogle ScholarPubMed
Andrews, A. T. 1978 The Composition, Structure and Origin of Proteose-peptone Component 5 of Bovine Milk. European Journal of Biochemistry 90 5965CrossRefGoogle ScholarPubMed
Aso, K., Yamashita, M., Arai, S. & Fujimaki, M. 1973 General Properties of a Plastein Synthesised from a Soybean Protein Hydrolysate. Agricultural and Biological Chemistry 37 25052509CrossRefGoogle Scholar
Edwards, J. H. & Shipe, W. F. 1978 Characterization of Plastein Reaction Products Formed by Pepsin, α-Chymotrypsin and Papain Treatments of Egg Albumin Hydrolysates. Journal of Food Science 43 12151218CrossRefGoogle Scholar
Eriksen, S. & Fagerson, I. S. 1976 The Plastein Reaction and Its Applications: A Review. Journal of Food Science 41 490493CrossRefGoogle Scholar
Fujimaki, M., Arai, S. & Yamashita, M. 1977 Enzymatic Protein Degradation and Resynthesis for Protein Improvement. In Food Proteins: Improvement Through Chemical and Enzymatic Modification pp. 156184 (Eds Feeney, R. E. and Whitaker, J. R.), Washington. DC: American Chemical SocietyCrossRefGoogle Scholar
Fujimaki, M., Kato, H., Arai, S. & Yamashita, M. 1971 Application of Microbial Proteases to Soybean and Other Materials to Improve Acceptability, Especially through Formation of Plastein. Journal of Applied Bacteriology 34 119131CrossRefGoogle ScholarPubMed
Horowitz, J. & Haurowitz, F. 1959 Mechanism of Plastein Formation. Biochimica el Biophysica Acta 33 231237.CrossRefGoogle ScholarPubMed
Sukan, G. & Andrews, A. T. 1982 Application of the Plastein Reaction to Caseins and to Skim-Milk Powder. I. Protein Hydrolysis and Plastein Formation. Journal of Dairy Research 49 265278CrossRefGoogle Scholar
Taylor, M. D. & Andrews, A. T. 1981 Rapid and Sensitive Location of Protein Zones in Gels using o-Phthaldialdehyde. Electrophoresis 2 7681CrossRefGoogle Scholar
Tsai, S. J., Yamishita, M., Arai, S. & Fujimaki, M. 1974 Polyacrylamide Gel Electrophoresis of Plasteins. Agricultural and Biological Chemistry 38 641644CrossRefGoogle Scholar
Von Hofsten, B. 1974 Enzymatisk Hydrolys av Näringsproteiner. STU report no. 733, 229, University of Uppsala, SwedenGoogle Scholar
Von Hofsten, B. & Lalasidis, G. 1976 Protease-catalyzed Formation of Plastein Products and some of their Properties. Journal of Agricultural and Food Chemistry 24 460465CrossRefGoogle ScholarPubMed