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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
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: [email protected]

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
Copyright
Copyright © Cambridge University Press 2013 

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