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Ruminal dry matter and nitrogen degradation in relation to condensed tannin and protein molecular structures in sainfoin (Onobrychis viciifolia) and lucerne (Medicago sativa)

Published online by Cambridge University Press:  29 July 2013

J. AUFRÈRE ,
K. THEODORIDOU ,
I. MUELLER-HARVEY ,
P. YU  and
D. ANDUEZA
J. AUFRÈRE
Affiliation:
INRA, UMR1213 Herbivores, F-63122 Saint-Genès Champanelle, France Clermont Université, VetAgro Sup, UMR Herbivores, BP 10448, F-63000, Clermont-Ferrand, France
K. THEODORIDOU
Affiliation:
Department of Animal and Poultry Science, College of Agriculture and Bioresources, University of Saskatchewan, 51 Campus Drive, Saskatoon, SK S7N 5A8, Canada
I. MUELLER-HARVEY
Affiliation:
Chemistry and Biochemistry Laboratory, Division of Food Production and Quality, School of Agriculture, Policy and Development, University of Reading, Reading RG6 6AT, UK
P. YU
Affiliation:
Department of Animal and Poultry Science, College of Agriculture and Bioresources, University of Saskatchewan, 51 Campus Drive, Saskatoon, SK S7N 5A8, Canada
D. ANDUEZA*
Affiliation:
INRA, UMR1213 Herbivores, F-63122 Saint-Genès Champanelle, France Clermont Université, VetAgro Sup, UMR Herbivores, BP 10448, F-63000, Clermont-Ferrand, France
*
*To whom all correspondence should be addressed. Email: donato.andueza@clermont.inra.fr
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Summary

Sainfoin is a temperate legume that contains condensed tannins (CT), i.e. polyphenols that are able to bind proteins and thus reduce protein degradation in the rumen. A reduction in protein degradation in the rumen can lead to a subsequent increase in amino acid flow to the small intestine. The effects of CT in the rumen and the intestine differ according to the amount and structure of CT and the nature of the protein molecular structure. The objective of the present study was to investigate the degradability in the rumen of three CT-containing sainfoin varieties and CT-free lucerne in relation to CT content and structure (mean degree of polymerization, proportion of prodelphinidins and cis-flavanol units) and protein structure (amide I and II bands, ratio of amide I-to-amide II, α-helix, β-sheet, ratio of α-helix-to-β-sheet). Protein molecular structures were identified using Fourier transform/infrared-attenuated total reflectance (FT/IR-ATR) spectroscopy. The in situ degradability of three sainfoin varieties (Ambra, Esparcette and Villahoz) was studied in 2008, during the first growth cycle at two harvest dates (P1 and P2, i.e. 5 May and 2 June, respectively) and at one date (P3) during the second growth cycle (2 June) and these were compared with a tannin-free legume, lucerne (Aubigny). Loss of dry matter (DMDeg) and nitrogen (NDeg) in polyester bags suspended in the rumen was measured using rumen-fistulated cows. The NDeg of lucerne compared with sainfoin was 0·80 v. 0·77 at P1, 0·78 v. 0·65 at P2 and 0·79 v. 0·70 at P3, respectively. NDeg was related to the rapidly disappearing fraction (‘a’) fraction (r=0·76), the rate of degradation (‘c’) (r=0·92), to the content (r=−0·81) and structure of CT. However, the relationship between NDeg and the slowly disappearing fraction (‘b’) was weak. There was a significant effect of date and species×date, for NDeg and ‘a’ fraction. The secondary protein structure varied with harvest date (species×date) and was correlated with the fraction ‘b’. Both tannin and protein structures influenced the NDeg degradation. CT content and structure were correlated to the ‘a’ fraction and to the ‘c’. Features of the protein molecular secondary structure were correlated to the ‘b’ fraction.

Type
Animal Research Papers
Information
The Journal of Agricultural Science , Volume 152 , Issue 2 , April 2014 , pp. 333 - 345
Copyright
Copyright © Cambridge University Press 2013 

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References

Aufrère, J. & Michalet-Doreau, B. (1985). In vivo digestibility and prediction of digestibility of some by-products. In Feeding Value of By-products and their Use by Beef Cattle (Eds Boucqué, C. H. V., Fiems, L. O. & Cottyn, B. G.), pp. 25–33. Report EUR 8918 EN. Brussels, Luxembourg: Office for Official Publications of the European Communities.Google Scholar
Aufrère, J., Boulberhane, D., Graviou, D. & Demarquilly, C. (1994). Comparison of in situ degradation of cell-wall constituents, nitrogen and nitrogen linked to cell walls for fresh lucerne and 2 lucerne silages. Annales de Zootechnie 43, 125–134.CrossRefGoogle Scholar
Aufrère, J., Dudilieu, M. & Poncet, C. (2008). In vivo and in situ measurements of the digestive characteristics of sainfoin in comparison with lucerne fed to sheep as fresh forages at two growth stages and as hay. Animal 2, 1331–1339.CrossRefGoogle ScholarPubMed
Aufrère, J., Dudilieu, M., Andueza, D., Poncet, C. & Baumont, R. (2013). Mixing sainfoin and lucerne to improve the feed value of legumes fed to sheep by the effect of condensed tannins. Animal 7, 82–92.Google Scholar
Azuhnwi, B. N., Thomann, B., Arrigo, Y., Boller, B., Hess, H. D., Kreuzer, M. & Dohme-Meier, F. (2012). Ruminal dry matter and crude protein degradation kinetics of five sainfoin (Onobrychis viciifolia Scop) accessions differing in condensed tannin content and obtained from different harvests. Animal Feed Science and Technology 177, 135–143.CrossRefGoogle Scholar
Barth, A. (2007). Infrared spectroscopy of proteins. Biochimica et Biophysica Acta – Bioenergetics 1767, 1073–1101.Google Scholar
Budevska, B. O. (2002). Applications of vibrational spectroscopy in life, pharmaceutical and natural sciences. In Handbook of Vibrational Spectroscopy (Eds Chalmers, J. M. & Griffiths, P. R.), pp. 3720–3732. New York: John Wiley & Sons.Google Scholar
Dobreva, M. A., Frazier, R. A., Mueller-Harvey, I., Clifton, L. A., Gea, A. & Green, R. J. (2011). Binding of pentagalloyl glucose to two globular proteins occurs via multiple surface sites. Biomacromolecules 12, 710–715.Google Scholar
Doiron, K., Yu, P., Mckinnon, J. J. & Christensen, D. A. (2009). Heat-induced protein structure and subfractions in relation to protein degradation kinetics and intestinal availability in dairy cattle. Journal of Dairy Science 92, 3319–3330.Google Scholar
Frazier, R. A., Papadopoulou, A., Mueller-Harvey, I., Kissoon, D. & Green, R. J. (2003). Probing protein–tannin interactions by isothermal titration microcalorimetry. Journal of Agricultural and Food Chemistry 51, 5189–5195.CrossRefGoogle ScholarPubMed
Frutos, P., Hervas, G., Giraldez, F. J. & Mantecon, A. R. (2004). Review. Tannins and ruminant nutrition. Spanish Journal of Agricultural Research 2, 191–202.Google Scholar
Gea, A., Stringano, E., Brown, R. H. & Mueller-Harvey, I. (2011). In situ analysis and structural elucidation of sainfoin (Onobrychis viciifolia) tannins for high throughput germplasm screening. Journal of Agricultural and Food Chemistry 59, 495–503.Google Scholar
Guimaraes-Beelen, P. M., Berchielli, T. T., Beelen, R. & Medeiros, A. N. (2006). Influence of condensed tannins from Brazilian semi-arid legumes on ruminal degradability, microbial colonization and ruminal enzymatic activity in Saanen goats. Small Ruminant Research 61, 35–44.CrossRefGoogle Scholar
Himmelsbach, D. S., Khalili, S. & Akin, D. E. (1998). FT-IR microspectroscopic imaging of flax (Linum usitatissimum L.) stems. Cellular and Molecular Biology 44, 99–108.Google Scholar
Jackson, M. & Mantsch, H. H. (2000). Ex vivo tissue analysis by infrared spectroscopy. In Encyclopedia of Analytical Chemistry (Ed. Meyers, R. A.), pp. 131–156. Chichester, UK: John Wiley & Sons.Google Scholar
Kemp, W. (1991). Organic Spectroscopy. New York: W. H. Freeman.Google Scholar
Koupai-Abyazani, M. R., Mccallum, J., Muir, A. D., Bohm, B. A., Towers, G. H. N. & Gruber, M. Y. (1993). Developmental changes in the composition of proanthocyanidins from leaves of sainfoin (Onobrychis viciifolia Scop.) as determined by HPLC analysis. Journal of Agricultural and Food Chemistry 41, 1066–1070.CrossRefGoogle Scholar
Mangan, J. L. (1982). The nitrogenous constituents of fresh forages. In Forage Protein in Ruminant Animal Production (Eds Thomson, D. J., Beever, D. E. & Gunn, R. G.), pp. 25–40. Occasional Publication No 6. Edinburgh, UK: British Society of Animal Production.Google Scholar
McAllister, T. A., Martinez, T., Bae, H. D., Muir, A. D., Yanke, L. J. & Jones, G. A. (2005). Characterization of condensed tannins purified from legume forages: chromophore production, protein precipitation and inhibitory effects on cellulose digestion. Journal of Chemical Ecology 31, 2049–2068.CrossRefGoogle ScholarPubMed
Mehansho, H., Butler, L. G. & Carlson, D. M. (1987). Dietary tannins and salivary proline-rich proteins: interactions, induction and defense mechanisms. Annual Review of Nutrition 7, 423–440.Google Scholar
Miller, L. M. & Dumas, P. (2010). From structure to cellular mechanism with infrared microspectroscopy. Current Opinion in Structural Biology 20, 649–656.Google Scholar
Min, B. R., Mcnabb, W. C., Barry, T. N. & Peters, J. S. (2000). Solubilization and degradation of ribulose-1-5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39; Rubisco) protein from white clover (Trifolium repens) and Lotus corniculatus by rumen microorganisms and the effect of condensed tannins on these processes. Journal of Agricultural Science, Cambridge 134, 305–317.CrossRefGoogle Scholar
Min, B. R., Barry, T. N., Attwood, G. T. & Mcnabb, W. C. (2003). The effect of condensed tannins on the nutrition and health of ruminants fed fresh temperate forages: a review. Animal Feed Science and Technology 106, 3–19.Google Scholar
Mueller-Harvey, I. (2006). Unravelling the conundrum of tannins in animal nutrition and health. Journal of Science of Food and Agriculture 86, 2010–2037.CrossRefGoogle Scholar
Nugent, J. H. A. & Mangan, J. L. (1981). Characteristics of the rumen proteolysis of fraction I (18S) leaf protein from lucerne. British Journal of Nutrition 46, 39–58.Google Scholar
Ørskov, E. R. & 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.Google Scholar
Pagan, S., Wolfe, R. M., Terrill, T. H. & Muir, J. P. (2009). Effect of drying method and assay methodology on detergent fiber analysis in plants containing condensed tannins. Animal Feed Science and Technology 154, 119–124.Google Scholar
Reed, J. D. (1986). Relationships among phenolics, insoluble proanthocyanidins and fiber in East African browse species. Journal of Range Management 39, 5–7.Google Scholar
Samadi, Theodoridou K. & Yu, P. (2013). Detect the sensitivity and response of protein molecular structure of whole canola seed (yellow and brown) to different heat processing methods and relation to protein utilization and availability using ATR-FT/IR molecular spectroscopy with chemometrics. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 105, 304–313.Google Scholar
Sanderson, M. A. & Wedin, W. F. (1989). Nitrogen in the detergent fibre fractions of temperate legumes and grasses. Grass and Forage Science 44, 159–168.Google Scholar
SAS Institute Inc (2000). SAS/STAT Guide for Personal Computers, Version 8.0. Cary, NC: SAS Institute.Google Scholar
Stringano, E., Hayot Carbonero, C., Smith, L. M. J., Brown, R. H. & Mueller-Harvey, I. (2012). Proanthocyanidin diversity in the EU ‘HealthyHay’ sainfoin (Onobrychis viciifolia) germplasm collection. Phytochemistry 77, 197–208.Google Scholar
Theodoridou, K., Aufrère, J., Andueza, D., Pourrat, J., Le Morvan, A., Stringano, E., Mueller- Harvey, I. & Baumont, R. (2010). Effects of condensed tannins in fresh sainfoin (Onobrychis viciifolia) on in vivo and in situ digestion in sheep. Animal Feed Science and Technology 160, 23–28.Google Scholar
Theodoridou, K., Aufrère, J., Andueza, D., Le Morvan, A., Picard, F., Stringano, E., Pourrat, J., Mueller-Harvey, I. & Baumont, R. (2011). Effect of plant development during first and second growth cycle on chemical composition, condensed tannins and nutritive value of three sainfoin (Onobrychis viciifolia) varieties and Lucerne. Grass and Forage Science 66, 402–414.Google Scholar
Van Soest, P. J. (1994). Nitrogen metabolism. In Nutritional Ecology of the Ruminant, 2nd edn (Ed. Van Soest, P. J.), pp. 290–311. Ithaca, NY: Cornell University Press.Google Scholar
Van Soest, P. J. & Wine, R. H. (1967). Use of detergents in the analysis of fibrous feeds. IV Determination of plant cell-wall constituents. Journal of the Association of Official Analytical Chemists 50, 50–55.Google Scholar
Waghorn, G. (2008). Beneficial and detrimental effects of dietary condensed tannins for sustainable sheep and goat production. Progress and challenges. Animal Feed Science and Technology 147, 116–139.Google Scholar
Wetzel, D. L., Eilert, A. J., Pietrzak, L. N., Miller, S. S. & Sweat, J. A. (1998). Ultraspatially-resolved synchrotron infrared microspectroscopy of plant tissue in situ. Cellular and Molecular Biology (Noisy-le-Grand) 44, 145–168.Google Scholar
Wetzel, D. L., Srivarin, P. & Finney, J. R. (2003). Revealing protein infrared spectral detail in a heterogeneous matrix dominated by starch. Vibrational Spectroscopy 31, 109–114.Google Scholar
Yu, P. (2005). Protein secondary structures (α-helix and β-sheet) at a cellular level and protein fractions in relation to rumen degradation behaviours of protein: a new approach. British Journal of Nutrition 94, 655–665.Google Scholar
Yu, P. (2006). Synchrotron IR microspectroscopy for protein structure analysis: potential and questions. Spectroscopy 20, 229–251.Google Scholar
Yu, P. (2007). Molecular chemical structure of barley proteins revealed by ultra-spatially resolved synchrotron light sourced FTIR microspectroscopy: comparison of barley varieties. Biopolymers 85, 308–317.Google Scholar
Yu, P. (2010). Plant-based food and feed protein structure changes induced by gene-transformation, heating and bio-ethanol processing: a synchrotron-based molecular structure and nutrition research program. Molecular Nutrition and Food Research 54, 1535–1545.Google Scholar
Yu, P., Niu, Z. & Damiran, D. (2010). Protein molecular structures and protein fraction profiles of new coproducts from bioethanol production. A novel approach. Journal of Agricultural and Food Chemistry 58, 3460–3464.Google Scholar