Hostname: page-component-78c5997874-4rdpn Total loading time: 0 Render date: 2024-11-10T16:49:43.217Z Has data issue: false hasContentIssue false
  • English
  • Français

Effects of microwave irradiation on ruminal degradation and in vitro digestibility of soya-bean meal

Published online by Cambridge University Press:  09 March 2007

A. A. Sadeghi ,
A. Nikkhah  and
P. Shawrang
A. A. Sadeghi*
Affiliation:
Department of Animal Science, Faculty of Agriculture, Science and Research Campus, Islamic Azad University, PO Box 14155·4933, Tehran, Iran
A. Nikkhah
Affiliation:
Department of Animal Science, Faculty of Agriculture, Tehran University, PO Box 4111, Karaj, Iran
P. Shawrang
Affiliation:
Department of Animal Science, Faculty of Agriculture, Tehran University, PO Box 4111, Karaj, Iran
*
†E-mail: maryamsa1381@yahoo.com
Get access

Abstract

This study was carried out to determine ruminal dry matter (DM) and crude protein (CP) degradation characteristics of untreated, 2-, 4- and 6-min microwave-treated soya-bean meal (SBM) by using nylon bags and sodium dodecyl sulphatepolyacrylamide gel electrophoresis (SDS-PAGE) techniques. Nylon bags of untreated or treated SBM were suspended into the rumen of three Holstein steers from 0 to 48 h, and data were fitted to non-linear degradation characteristics to calculate effective rumen degradation (ERD). There were significant differences (P < 0·05) for DM and CP degradation parameters between untreated and microwave-treated SBM. Microwave treatments decreased the water-soluble fraction and increased the potentially degradable fraction of CP. The degradation rate of the latter fraction decreased with these treatments. As a consequence, microwave treatments decreased (P < 0·05) ERD of CP. From densitometric scanning, SBM proteins were seen to be composed of two major components; β-conglycinin and glycinin, accounting for proportionately 0·30 and 0·40 of buffer-soluble SBM proteins, respectively. Electrophoretic analysis of untreated, 2-, 4- and 6-min microwave-treated SBM protein residues revealed that two of the subunits of β-conglycinin (α -and α) were degraded completely after 2, 4, 24 and 48 h, respectively, whereas the α subunit of this protein was more resistant to degradation. In untreated SBM, the two subunits of glycinin (acidic and basic polypeptides) were degraded in the middle of the incubation period, but in microwave-treated SBM were not degraded until 48 h of incubation. In vitro digestibility of ruminally undegraded CP of untreated and treated SBM increased (P < 0·05) with increases in rumen incubation time from 8 to 24 h. In conclusion, SBM proteins appeared to be effectively protected from ruminal degradation by a 4-min microwave treatment. SDS-PAGE results indicated that ruminally undegraded protein from untreated SBM was mainly composed of the basic subunit of glycinin, whereas that from microwave-treated SBM was composed of β-conglycinin and both basic and acidic subunits of glycinin.

Keywords

microwave treatmentprotein degradationSDS-PAGEsoya-bean oilmeal
Type
Research Article
Information
Animal Science , Volume 80 , Issue 3 , June 2005 , pp. 369 - 375
Copyright
Copyright © British Society of Animal Science 2005

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

Agricultural and Food Research Council. 1993. Energy and protein requirements of ruminants. AFRC Technical Committee on Responses to Nutrients. CAB International, Wallingford.Google Scholar
Alton, W. J. 1998. Microwave pasteurization of liquids. Engineering Paper 2: 98–211.Google Scholar
Association of Official Analytical Chemists. 1995. Official methods of analysis, 16th edition. AOAC, Arlington, VA.Google Scholar
Banik, S., Bandyopadhyay, S. and Ganguly, S. 2003. Bio-effects of microwave. Bio-resource Technology 87: 155–159.CrossRefGoogle Scholar
Bjarnason, J. and Carpenter, K. J. 1969. Mechanisms of heat damage in protein. I. Model with acetylated lysine units. British Journal of Nutrition 23: 858–868.Google Scholar
Bradley, R. A., Atkinson, D., Hauser, H. H., Oldani, D., Green, J. P. and Stubbs, J. M. 1975. The structure, physical and chemical properties of the soya bean protein glycinin. Biochimica et Biophysica Acta 412: 214–228.Google Scholar
Calsamiglia, S. and Stern, M. D. 1995. A three-step in vitro procedure for estimating intestinal digestion of protein in ruminants. Journal of Animal Science 73: 1459–1465.CrossRefGoogle ScholarPubMed
Demjanec, B., Merchen, N. R., Cremin, J. D., Aldrich, C. G. and Berger, L. I. 1995. Effect of roasting on site and extent of digestion of soyabean meal by sheep. I. Digestion of nitrogen and amino acids. Journal of Animal Science 73: 824–834.CrossRefGoogle ScholarPubMed
Fakhouri, M. O. and Ramaswamy, H. S. 1993. Temperature uniformity of microwave heated foods as influenced by product type and composition. Food Research International 26: 89–95.CrossRefGoogle Scholar
Hu, B. and Esen, A. 1981. Heterogeneity of soybean seed proteins: one-dimensional electrophoretic pro. les of six different solubility fractions. Journal of Agricultural Food Chemistry 29: 497–501.CrossRefGoogle Scholar
Hvelplund, T., Weisbjerg, M. R. and Andersen, L. S. 1992. Estimation of the true digestibility of rumen-undegraded dietary protein in the small intestine of ruminants by the mobile bag technique. Acta Agriculturæ Agricultur Scandinavica, Section A-Animal Science 42: 34–39.Google Scholar
Kinsella, J. E. 1979. Functional properties of soy proteins. Journal of American Oil Chemistry Society 56: 242–258.CrossRefGoogle Scholar
Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.CrossRefGoogle ScholarPubMed
Langan, J. L. 1972. Quantitative studies on nitrogen metabolism in the bovine rumen. British Journal of Nutrition 27: 261–283.Google Scholar
Lynch, G. L., Berger, L. L. and Fahey, G. C. Jr 1987. Effects of ethanol, heat, and lipid treatment of soybean meal on nitrogen utilization by ruminants. Journal of Dairy Science 70: 90–97.Google ScholarPubMed
Mujoo, R. and Trinh, D. 2003. Characterization of storage proteins in different soybean varieties and their relationship to tofu yield and texture. Food Chemistry 82: 265–273.CrossRefGoogle Scholar
National Research Council. 1996. Nutrient requirement of beef cattle, sixth edition. National Academic Press, Washington, DC.Google Scholar
Oliveira, M. E. C. and Franca, A. S. 2002. Microwave heating of foodstuffs. Journal of Food Engineering 53: 347–359.CrossRefGoogle Scholar
Ørskov, E. R. 1992. Protein nutrition in ruminants. Academic Press, London.Google Scholar
Ørskov, E. R. and McDonald, I. 1979. The estimation of protein degradability in the rumen from incubation measurements weighted according to rate of passage. Journal of Agricultural Science, Cambridge 92: 499–503.CrossRefGoogle Scholar
Peng, I. C., Dayton, W. R., Quass, D. W. and Allen, C. E. 1982. Investigations of soybean 11S protein and myosin interaction by solubility, turbidity and titration studies. Journal of Food Science 47: 1976–1988.CrossRefGoogle Scholar
Romagnolo, E., Polan, C. E. and Barbeau, W. E. 1990. Degradability of soybean meal protein fractions as determined by dodecyl sulfatepolyacrylamide gel electrophoresis. Journal of Dairy Science 73: 2379–2385.CrossRefGoogle Scholar
Satter, L. D. 1986. Protein supply from undegraded dietary protein. Journal of Dairy Science 69: 2734–2749.Google ScholarPubMed
Statistical Analysis Systems Institute. 1996. User's guide. SAS Institute, Cary, NC.Google Scholar
Steel, R. G. D. and Torrie, J. H. 1980. Principles and procedures of statistics: a biometrical approach, second edition. McGraw Hill, New York, NY.Google Scholar
Thanh, V. H. and Shibasaki, K. 1976. Heterogeneity of betaconglycinin. Biochimica et Biophysica Acta 439: 326–338.CrossRefGoogle ScholarPubMed
Utsumi, S., Iuaba, H. and Mori, T. 1981. Heterogeneity of soybean glycinin. Phytochemistry 20: 585–593.CrossRefGoogle Scholar
Utsumi, S. and Kinsella, J. E. 1985. Structure-function relationship in food proteins: subunit interactions in heat-induced gelation of 7S, 11S and soy isolate proteins. Journal of Agricultural Food Chemistry 33: 297–303.CrossRefGoogle Scholar
Van der Aar, P. J., Berger, L. L., Wujek, K. M., Mastenbroek, I. and Fahey, G. C. 1983. Relationship between electrophoretic band patterns and in vitro ammonia release of soluble soybean meal protein. Journal of Dairy Science 66: 1270–1276.CrossRefGoogle Scholar
Van Soest, P. J., Robertson, J. B. and Lewis, B. A. 1991. Methods for dietary fiber, neutral detergent fiber and non-starch polysaccharides in relation to animal nutrition. Journal of Dairy Science 74: 3583–3597.CrossRefGoogle Scholar
Volden, H. and Harstad, O. M. 1995. Effect of rumen incubation on the true indigestibility of feed protein in the digestive tract determined by nylon bag techniques. Acta Agriculturæ Agricultur Scandinavica, Section A-Animal Science 45: 106–115.Google Scholar
Waltz, D. M. and Stern, M. D. 1989. Evaluation of various methods for protecting soya-bean protein from degradation by rumen bacteria. Animal Feed Science and Technology 25: 111–122.CrossRefGoogle Scholar
Weisbjerg, M. R., Bargava, P. K., Hvelplund, T. and Madsen, J. 1990. Use of degradation profiles in feed evaluation. Report of the National Institute of Animal Science, Frederiksberg.Google Scholar