S. Boisen et Ja. Fernandez, PREDICTION OF THE APPARENT ILEAL DIGESTIBILITY OF PROTEIN AND AMINO-ACIDS IN FEEDSTUFFS AND FEED MIXTURES FOR PIGS BY IN-VITRO ANALYSES, Animal feed science and technology, 51(1-2), 1995, pp. 29-43
An in vitro method for the prediction of protein and amino acid digest
ibility at ileal level is described. Values of in vitro digestibility
of protein in 15 common feedstuffs were an higher than corresponding v
alues of apparent ileal digestibility. The difference is suggested to
correspond to endogenous protein losses (EPL). A close relationship be
tween EPL and in vitro undigested dry matter (UDM) was demonstrated: E
PL, g kg(-1) DM intake=13.2+0.066 X UDM, g kg(-1) DM (n=15; r(2)=0.61;
RSD=4.5; CV=17.1). The prediction of apparent ileal digestibility of
protein (pdN(ileal)) by using the equation: pdN(ileal), %=dN(in vitro)
, %-100 X (13.2+0.066 X UDM, g kg(-1) DM)/Protein-(feed), g kg(-1) DM,
was highly related to the in vivo determined ileal digestibility of p
rotein (r(2)=0.92; RSD=3.5; CV=4.9) in the same 15 feedstuffs. The met
hod was validated with 48 feed mixtures with known in vivo digestibili
ty. The relationship was considerably lower (r(2)=0.57), which was par
tly due to the narrow variation range in protein digestibility in vivo
. The in vitro digestibility of amino acids (measured in nine feedstuf
fs) was in general closely related to that of protein. Exceptions were
cystine, arginine, aspartic acid, glutamic acid and proline. The endo
genous losses of the individual amino acids were calculated in a simil
ar way as described for EPL. The resulting amino acid composition of t
he endogenous protein was very close to reported values in the literat
ure based on direct measurements in vivo. Apparent ileal digestibility
of the individual amino acids was predicted in a similar way as descr
ibed for protein. The relationship was generally higher for essential
amino acids, and generally lower for non-essential amino acids, than f
or protein (e.g. r(2) values of 0.65, 0.71 and 0.77 was obtained for l
ysine, leucine and isoleucine, respectively, but 0.34 and 0.14 for glu
tamic acid and proline, respectively). The described in vitro approach
for protein evaluation seems to have a significant potential for prac
tical purposes.