Legume protein denaturation

From the nutritional point of view, denaturation is usually desirable since denatured proteins are more amenable to digestive enzymes than the native proteins. Denaturation, therefore, increases the bioavailabihty of proteins (e.g. sulfur-containing amino acids in cereals and legumes). Some antinutritional and natural toxic substances are also denatured, such as protease inhibitors (see Section 10.2.1.1), lectins (see Section 10.2.2.6), enzymes and other unwanted proteins and undesirable microorganisms. 

Lectins are another class of potential antinutrient soy proteins (Sharon Lis, 1972 Liener, 1974). The carbohydrate content and structure of soy lectins were determined (Lis Sharon, 1978) and consist of mannose and Af-acetyl-glucosamine at about 5% by weight. Soy lectin has MW 110 kD from four identical subunits. The soy lectins are partly responsible for weight loss in rodent feeding studies with raw soy protein. Soy lectins are relatively easy to heat denature compared to other legume lectins. Properly processed soy foods have little native lectin present. Soybean lectins are widely used in clinical studies because of their interaction with red blood cell surface features (Friedman Brandon, 2001). 

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