Total N-acetyl-D-galactosamine binding and functional brush border agglutin
ating lectins were measured in raw defatted soybean meal, in 11 samples of
soybean meals obtained from various processing plants using conventional de
solventising and toasting, and one sample of meal from a plant using a 'fla
sh' desolventising system. Agglutination activity of the affinity purified
lectins was measured with brush border vesicles prepared from the small int
estine of 4-week-old broiler chickens. Raw soybean meal contained 2.3 mg of
N-acetyl-D-galactosamine binding and 2.3 mg of brush border agglutinating
lectin protein/g. As such all of the lectin in the raw soybean meal retaine
d functional brush border agglutinating activity. Of the 11 samples of conv
entionally-processed soybean meal, three had 20-30%, six had 10-20%, and tw
o had 3-10%, of the concentration of carbohydrate-binding lectin obtained p
er gram of raw soybean meal. All the 11 samples had agglutinating lectin le
vels of less than 10% and eight had agglutinating levels of less than 3% of
the level found in raw soybean meal. The flash desolventised sample had a
carbohydrate binding lectin level in excess of that obtained with raw soybe
an meal and an agglutinating lectin level that was 38% of that obtained wit
h the raw meal. This study indicates that conventionally-processed soybean
meals can retain significant levels of carbohydrate-binding lectin but that
the functional capacity of the lectins to induce agglutination of the inte
stinal brush border membrane is mostly destroyed during processing. The fin
ding of substantial carbohydrate-binding lectin in some of the conventional
ly-processed samples, and of substantial carbohydrate-binding and brush bor
der agglutinating lectin in the flash desolventised sample suggests that so
ybean meals can, on occasion, retain functional lectins at levels that may
be detrimental to the animal's health and productivity. (C) 1999 Elsevier S
cience B.V.