Hostname: page-component-cd9895bd7-gxg78 Total loading time: 0 Render date: 2024-12-22T15:13:52.578Z Has data issue: false hasContentIssue false
  • English
  • Français

Extraction methods and test techniques for detection of vegetable proteins in meat products:I. Qualitative detection of soya derivatives

Published online by Cambridge University Press:  15 May 2009

N. ST G. Hyslop
N. ST G. Hyslop
Affiliation:
Animal Pathology Division, Health of Animals Branch, Agriculture Canada, Animal Diseases Research Institute (E), P.O. Box 11300, Postal Station H, Ottawa, Ontario, Canada, K2H 8P9
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Extracts of 3 soya bean preparations, used commercially in certain countries to replace part of the meat in popular meat products, were made by treatment with (i) sodium dodecyl sulphate, (ii) Triton-X100 or (iii) n–Butanol. Similar extracts were made from beef and pork.

All extracts were examined by electrophoretic and immunological techniques. Stained polyacrylamide gels revealed distinctive protein bands after electrophoresis. The migration rates of corresponding bands differed between beef and pork extracts. However, the migration rates of vegetable bands revealed certain similarities, but differed very greatly from those of animal origin. Characteristic fast-migrating S-bands were distinguishable only in extracts of vegetable protein. Immunodiffusion tests, using antisera produced in rabbits against each extract, revealed varying degrees of similarity between extracts of vegetable origin, but the antisera were specific for either vegetable or animal protein.

Type
Research Article
Information
Journal of Hygiene , Volume 76 , Issue 3 , June 1976 , pp. 329 - 336
Copyright
Copyright © Cambridge University Press 1976

References

REFERENCES

Balant, L., Mulli, J. C. & Fabre, J. (1974). Urinary protein analysis with sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Clinica chimica acta 54, 27–37.Google Scholar
Bjerrum, O. J. & Lindahl, P. (1974). Crossed immunoelectrophoresis of human erythrocyte membrane proteins. Biochimica et biophysica acta 342, 69–80.CrossRefGoogle ScholarPubMed
Cartwright, Sheila F. & Thorne, H. V. (1958). Some applications of detergents to the study of the virus of foot and mouth disease. Journal of General Microbiology 20, 61–77.CrossRefGoogle Scholar
Frouin, A. (1974). Detection of soy proteins. Journal of the American Oil Chemists' Society 51, 188A–89A.Google Scholar
Hyslop, N. St G. (1972). Application of an improved system of electrophoresis in acrylamide gel to studies on the sera of different species. Journal of Clinical Pathology 25, 508–11.Google Scholar
Hyslop, N. St G. (1973). Effect of dextrans of different mean molecular weights on immuno-diffusion reactions of serum fractions. Journal of Chromatography 77, 445–9.CrossRefGoogle Scholar
Hyslop, N. St G. & Cochrane, Delma G. (1974). Effects of dextrans on immunoprecipitation in agar and in low-temperature-gelling agarose gels. Journal of Immunological Methods 6, 99–107.Google Scholar
Shapiro, A. L., Vinuela, E. & Maizel, J. V. (1967). Molecular weight estimation of poly-peptide chains by electrophoresis in SDS-polyacrylamide gels. Biochemical and Biophysical Research Communications 28, 815–20.CrossRefGoogle Scholar
Wilding, M. S. (1974). Textured proteins in meats and meat-like products. Journal of the American Oil Chemists' Society 51, 128A–30A.Google Scholar