Effect of Processing on Protein Utilization by Ruminants

  • Glen A. Broderick
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 86)

Abstract

Processing with heat or chemical reagents will reduce protein digestibility by reducing protein solubility in digestion media, due in part to crosslinking of peptide chains. This effect will have adverse effects on protein utilization by monogastric animals. However, processing may actually improve ruminant protein utilization by reducing ruminal microbial degradation, thereby increasing the proportion of dietary protein escaping to the small intestine for digestion there. Chemical treatments, particularly formaldehyde-treatment, have been used to obtain ruminai protein protection. Results with formaldehyde however, have not yielded consistent improvements in ruminant protein utilization, probably because proteins have been over-protected. Heat-treatments, such as those used during oil extraction from oilseed meals, will also increase ruminal protein escape or by-pass. Experimental results illustrating these effects were obtained with samples of “cold-extracted” cottonseed meal (CSM) which were subjected to graded levels of heat-processing by autoclaving for various lengths of time. Reaction of lysine ε-amino groups with carbohydrate and other compounds was assessed by ninhydrin assay on intact CSM samples. Also measured were N-solubilities in.02N NaOH, free gossypol content, in vitro ruminal degradation rate and estimated ruminai by-pass. Heat-treatment of CSM proteins was found to reduce solubility and ruminai degradation, with corresponding increases in estimated ruminai protein by-pass. Gossypol binding appeared to account for much of the loss of protein amino groups and possibly acted as a crosslinking agent, reducing ruminai solu-bility and therefore degradation. Other aspects of processing and ruminant protein nutrition are also discussed

Keywords

Cottonseed Meal Free Gossypol Protein Utilization Peanut Meal Texas Agricultural Experiment Station 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

  1. A.O.C.S. (1970). Official and tentative methods of the American Oil Chemists Society ( 3rd Ed ). Amer. Oil Chem. Soc., Champaign, Ill.Google Scholar
  2. Baliga, B. P. and Lyman, C. M. (1957). Preliminary report on the nutritional significance of bound gossypol in cottonseed meal. J. Amer. Oil Chem. Soc. 34: 21.CrossRefGoogle Scholar
  3. Beckwith, A. C., Paulis, J. W. and Wall, J. S. (1975). Direct estimation of lysine in corn meals by the ninhydrin color reaction. J. Agr. Food Chem. 23: 194.CrossRefGoogle Scholar
  4. Broderick, G. A. (1975). Factors affecting ruminant responses to protected amino acids and proteins. In M. Friedman (Ed.) Protein Nutritional Quality of Foods and Feeds. Vol. 1, Part 2. Marcel Dekker, Inc., New York.Google Scholar
  5. Broderick, G. A. (1976). Modification of an in vitro procedure for estimating ruminal protein by-pass. Fed. Proc. 35: 442 (Abstr.).Google Scholar
  6. Broderick, G. A., Kowalczyk, T., and Satter, L. D. (1970). Milk production response to supplementation with encapsulated methionine per os or casein per abomasum. J. Dairy Sci., 53: 1714.PubMedCrossRefGoogle Scholar
  7. Chalmers, M. I., Cuthbertson, D. P., and Synge, R. L. M. (1954). Ruminal ammonia formation in relation to the protein requirement of sheep. I. Duodenal administration and heat processing as factors influencing fate of casein supplements. J. Agr. Sci., 44: 254.CrossRefGoogle Scholar
  8. Chalupa, W. (1975). Rumen bypass and protection of proteins and amino acids. J. Dairy Sci. 58: 1198.PubMedCrossRefGoogle Scholar
  9. Chalupa, W., Chandler, J. E. and Brown, R. E. (1972). Amino acid nutrition of growing cattle. Fed. Proc., 31: 681 (Abstr.).Google Scholar
  10. Chalupa, W., Chandler, J. E. and Brown, R. E. (1973). Abomasal infusion of mixtures of amino acids to growing cattle. J. Anim. Sci., 37: 339 (Abstr.).Google Scholar
  11. Clark, J. H. (1975). Nitrogen metabolism in ruminants: Protein solubility and rumen bypass of protein and amino acids. In M. Friedman (Ed.) Protein Nutritional Quality of Foods and Feeds. Vol. 1, Part 2. Marcel Dekker, Inc., New York.Google Scholar
  12. Derrig, R. G., Clark, J. H. and Davis, C. L. (1974). Effect of abomasal infusion of sodium caseinate on milk yield, nitrogen utilization and amino acid nutrition of the dairy cow. J. Nutr., 104: 151.PubMedGoogle Scholar
  13. Faichney, G. J. and Davies, H. L. (1972). The effect of formaldehyde treatment of peanut meal in concentrate diets on the performance of calves. Australian J. Agr. Res., 23: 167.CrossRefGoogle Scholar
  14. Ferguson, K. A., Hemsley, J. A. and Reis, P. J. (1967). The effect of protecting dietary protein from microbial degradation in the rumen. Australian J. Sci., 30: 215.Google Scholar
  15. Friedman, M. and Broderick, G. A. (1977). Protected proteins in ruminant nutrition: In vitro evaluation of casein derivatives. This volume.Google Scholar
  16. Glimp, H. A., Karr, M. R., Little, C. 0., Woolfolk, P. G., Mitchell, Jr., G. E. and Hudson, L. W. (1967). Effect of reducing soybean protein solubility by dry heat on the protein utilization of young lambs. J. Anim. Sci., 26: 858.PubMedGoogle Scholar
  17. Goering, H. K. and Waldo, D. R. (1974). Processing effects on protein utilization by ruminants. Proc. Cornell Nutr. Conf. p. 25.Google Scholar
  18. Henderickx, H. and Martin, J. (1963). In vitro study of nitrogen metabolism in the rumen. Compt. Rend. Rech., Inst. Rech. Sci. Ind. Agr., Bruxelles, 31:7.Google Scholar
  19. Hogan, J. P. (1975). Quantitive aspects of nitrogen utilization in ruminants. J. Dairy Sci., 58: 1164.PubMedCrossRefGoogle Scholar
  20. Hurrell, R. F. and Carpenter, K. J. (1977). Nutritional significance of cross-link formation during food processing. This volume.Google Scholar
  21. Hurrell, R. F., Carpenter, K. J., Sinclair, W. J., Otterburn, M. S. and Asquith, R. S. (1976). Mechanisms of heat damage in proteins. 7. The significance of lysine-containing isopeptides and of lanthionine in heated proteins. Brit. J. Nutr. 35: 383.PubMedCrossRefGoogle Scholar
  22. Lyman, C. M., Baliga, B. P., Slay, M. W. (1959). Reactions of proteins with gossypol. Arch. Biochem. Biophys., 84: 486.PubMedCrossRefGoogle Scholar
  23. Lyman, C. M., Chang, W. Y., and Couch, J. R. (1953). Evaluation of protein quality in cottonseed meals by chick growth and by a chemical index method. J. Nutr., 49: 679.PubMedGoogle Scholar
  24. Martinez, W. H., Berardi, L. C., Frampton, V. L., Wilcke, H. L., Greene,D. E., and Teichman, R. (1967). Importance of cellular constituents to cottonseed meal protein quality. J. Agr. Food Chem., 15: 427.Google Scholar
  25. Mowat, D. N. and Deelstra, K. (1972). Encapsulated methionine supplement for growing-finishing lambs. J. Anim. Sci., 34: 332.Google Scholar
  26. Ørskov, E. R. and Fraser, C. (1969). The effect on nitrogen retention in lambs of feeding protein supplements direct to the abomasum. Comparison of liquid and dry feeding and of various sources of protein. J. Agr. Sci., 73: 469.CrossRefGoogle Scholar
  27. Ørskov, E. R., Fraser, C., and Corse, E. L. (1970). The effect on protein utilization of feeding different protein supplements via the rumen or via the abomasum in young growing sheep. Brit. J. Nutr., 24: 803.PubMedCrossRefGoogle Scholar
  28. Peter, A. P., Hatfield, E. E., Owens, F. N. and Garrigus, U. S. (1971). Effects of aldehyde treatments of soybean meal on in vitro ammonia release, solubility and lamb performance. J. Nutr. 101: 605.PubMedGoogle Scholar
  29. Reis, P. J., Schinckel, P. G. (1964). The growth and composition of wool. II. The effect of casein, gelatin and sulphur-containing amino acids given per abomasum. Aust. J. Biol. Sci., 17: 532.Google Scholar
  30. Schelling, G. T., Chandler, J. E. and Scott, G. C. (1973). Postruminal supplemental methionine infusion to sheep fed high quality diets. J. Anim. Sci., 37: 1034.PubMedGoogle Scholar
  31. Schelling, G. T. and Hatfield, E. E. (1968). Effect of abomasally infused nitrogen sources on nitrogen retention of growing lambs. J. Nutr. 96: 319.PubMedGoogle Scholar
  32. Schwab, C. G., Satter, L. D. and Clay, A. B. (1976). Response of lactating dairy cows to abomasal infusion of amino acids. J. Dairy Sci. 59: 1254.PubMedCrossRefGoogle Scholar
  33. Tagari, H., Ascarelli, I. and Bondi, A. (1962). The influence of heating on the nutritive value of soya-bean meal for ruminants. Brit. J. Nutr., 16: 237.PubMedCrossRefGoogle Scholar
  34. Vik-Mo, L., Emery, R. S. and Huber, J. T. (1974). Milk protein production in cows abomasally infused with casein or glucose. J. Dairy Sci., 57: 869.PubMedCrossRefGoogle Scholar
  35. Whitelaw, F. G. and Preston, T. R. (1963). The nutrition of the early-weaned calf. III. Protein solubility and amino acid composition as factors affecting protein utilization. Anim. Prod., 5: 131.Google Scholar
  36. Whitelaw, F. G., Preston, T. R. and Dawson, G. S. (1961). The nutrition of the early-weaned calf. II. A comparison of commercial groundnut meal, heat-treated groundnut meal and fish meal as the major protein source in the diet. Anim. Prod., 3: 127.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1977

Authors and Affiliations

  • Glen A. Broderick
    • 1
  1. 1.Department of Animal ScienceTexas A&M University and Texas Agricultural Experiment StationCollege StationUSA

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