Carbohydrate-binding and agglutinating lectins in raw and processed soybean meals

Citation
Dd. Maenz et al., Carbohydrate-binding and agglutinating lectins in raw and processed soybean meals, ANIM FEED S, 76(3-4), 1999, pp. 335-343
Citations number
12
Categorie Soggetti
Animal Sciences
Journal title
ANIMAL FEED SCIENCE AND TECHNOLOGY
ISSN journal
03778401 → ACNP
Volume
76
Issue
3-4
Year of publication
1999
Pages
335 - 343
Database
ISI
SICI code
0377-8401(199901)76:3-4<335:CAALIR>2.0.ZU;2-3
Abstract
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.