Variability of amino acid digestibility of lupin and pea grains in caecectomised laying hens

ABSTRACT

1. The objective of this study was to investigate the variations in amino acid (AA) digestibility of lupin and pea grains in caecectomised laying hens. The relationship between AA digestibility and chemical constituents of the grains was determined.

2. Twelve variants of lupins and peas were each added to a basal diet at a concentration of 300 g/kg, at the expense of maize starch. The lupin and pea variants were separately investigated in two subsequent trials. Each trial consisted of two 7 × 7 Latin squares, each comprising the basal diet and six diets with lupins or peas.

3. Fourteen caecectomised laying hens (LSL-classic) were individually housed in metabolism cages and 120 g/d of experimental diets were provided for eight days. During the last four days, excreta were collected quantitatively and feed intake was recorded. A regression approach was used to determine the AA digestibility of the lupin and pea variants.

4. Amino acid digestibility of the lupins and peas was high, although significant differences in AA digestibility among the lupins and peas were detected. The digestibility of lysine was in the range of 0.87–0.91 and 0.87–0.93 for lupins and peas, respectively. The digestibility of methionine in lupins and peas varied between 0.80–0.88 and 0.72–0.90. Variations in AA digestibility in peas were more pronounced than in lupins.

5. Significant correlations between chemical constituents of lupins, such as alkaloids, and AA digestibility were detected in some cases, without a consistent pattern. In peas, tannin concentration and the insoluble protein fraction were negatively correlated with digestibility of some AAs, but only when one colour flower variant was considered. Trypsin inhibitor activity in peas was negatively correlated with AA digestibility, particularly for the white flower variants.

KEYWORDS:

• Antinutritive factors
• poultry
• prediction
• protein
• pulses

Acknowledgements

The authors are grateful for the financial support given by the Union zur Förderung der Öl- und Proteinpflanzen (UFOP) e. V., Berlin, and for material support provided by Saatzucht Steinach GmbH & Co. KG and Norddeutsche Pflanzenzucht Hans-Georg Lembke KG. In addition, the authors wish to thank Michael Wink from the University of Heidelberg for the analyses of trypsin inhibitor activity in peas and alkaloids in lupins.

Disclosure statement

No potential conflict of interest was reported by the authors.

Supplementary material

Supplementary data for this article can be accessed here.