You seem to have problem with understanding that Soy Lecithin and Soy Lectins are entirely different things.
Soy lecithin is a mixture of fatty substances that are derived from the processing of soybeans. It is usually sold as a dietarry supplement that aids liver & gallbladder function and it prevents Gallstones
On the other side, Lectins are proteins commonly found in foods of high nutritional value, including all beans and also Soy beens.
Lectins can be good and bad ... depends when, and depends for who. Almost all foods that we consume contain some lectins, so just because foods contain lectins, it doesn't mean that it is bad.
What is soy lecithin? Is it safe for a soy-allergic individual?
Soy lecithin is a mixture of fatty substances that are derived from the processing of soybeans. The soybeans are initially tempered for 7 to 10 days during which time they are kept at a consistent temperature (75 degrees F) and moisture level. This process hydrates the beans and loosens the hull. The beans are then cleaned and cracked into small pieces by running the beans through a pair of sequential rollers. An air stream separates the hulls from the cracked beans. The soybeans are then steam heated to a temperature of 140 to 170 degrees F and pressed into flakes as they pass through a pair of rollers. The flakes enter the extractor where they are kept at 130 to 150 degrees F for the production of soybean oil, which is extracted through a distillation process.
Lecithin is separated from soybean oil by the addition of water and centrifugation (rapid spinning) and purified for use as a food additive. Its chemical name is phosphatidylcholine, which identifies its major components of choline, phosphoric acid, glycerin, and fatty acids. Lecithin is used widely in foods as an emulsifier, stabilizer, and antioxidant.
Studies show most soy-allergic individual can safely eat products containing soy lecithin without experiencing any allergic reactions. Discuss whether or not you should avoid soy lecithin with your primary allergist/pediatrician.
Adapted from food allergy
News, Volume 2, Number 1.
LECTINS AND MITOGENS
PETER J. D'ADAMO
Originally published in the Townsend Letter For Doctors, August 1990
Lectins are proteins commonly found In foods of high nutritional value. Typically, lectins interact with glycoprotein, glycolipid or oligosaccharide residues on the cell surface, causing a variety of effects including: blastogenesis (rapid cell reproduction), agglutination and receptor agonism. The mucin-rich gut wall is especially prone to direct reactions with lectin-containing foods in the diet.
Lectins (from the Latin legate, to pick or choose) were first identified in 1888 by Stillmark at the University of Dorpat in Estonia. While investigating the toxic effects on blood of castor bean extract (Ricinus communis) he noticed that the red cells were being agglutinated. He isolated the material responsible for the agglutination and called it ricin. Shortly afterward at the same university Helfin discovered that the toxic extract of the seed Abrus precatoris also caused cells to clump together. This new agglutinin was called abrin. This immediately caught the attention of the German bacteriologist Ehrlich who recognized that he could investigate certain immunologic problems with them rather than the then popular bacterial toxins. With these two agglutinins some of the most basic principles of immunology were discovered, such as antibody specificity and species specificity. In 1908 Landsteiner reported that small amounts of lentil lectin would agglutinate rabbit erythrocytes, even high concentrations of the lectin had no effect on pigeon red cells.
The first lectin to be purified was concanavallin-A, isolated from the jack bean. In 1936 Sumner and Howell noted that the addition of Con-A to a solution of glycogen caused the Sugar
to precipitate, and that the agglutination of red cells by this lectin was inhibited by cane sugar. They suggested that the hemagglutination by Con-A might be the consequence of a reaction between the protein with carbohydrates on the surface of the red cells. In other words lectins bind sugars, and they agglutinate cells by means of this binding. For example the agglutination of red cells by Con-A specifically inhibited by the sugars mannose or glucose, Indicating that Con-A binds mannose and glucose on the cell surface. It was soon discovered that lectins not only agglutinate red blood cells, but also other kinds of cells including lymphocytes, spermatozoa, bacteria and fungii.
There is some controversy over whether non-agglutinating (i.e. monovalent) molecules having high affinity for carbohydrate should be termed "lectins", however in this monograph they have been included, as many of these molecules, while not agglutinins, do have mitogenic propertles. In 1945 William Boyd of the Boston University School of Medicine discovered that lectins can be blood group specific; being able to agglutinate the red cells of one type but not those of another. He discovered that lima bean lectin would agglutinate red cells of human blood type A but not those of O or B. The seeds of Lotus tetragonobolus can agglutinate group O specifically, and Bandairaea simplicofolia is specific to group B. The specificity of lectins is so sharply defined that they can differentiate among blood subgroups. Dolichos biflorens lectin reacts more vigorously with blood group Al than A2. Other blood groups can be distinguished by lectins, such as M and N types, and lectins can help distinguish and diagnosis "secretors"; people who secrete glycoproteins that have blood-group specificity into their urine, saliva and other body fluids