The major protein of Great Northern beans was isolated through salt extraction, ammonium sulfate fractionation, gel filtration and DEAE‐cellulose ion exchange chromatography. Physicochemical properties of the major bean protein were determined. Results from heat stability studies showed that the protein was the most stable at pH values between 4 and 6. A complete unfolding of the bean protein was not essential in order to improve its digestibility. The native protein had a compact structure and therefore was resistant to the attack by proteolytic enzymes. A glycopeptide containing a N‐glycosidic protein‐carbohydrate linkage, isolated from a protease digestion of the major bean protein was also characterized. Results implied that the carbohydrate moeity might have a negative influence on the digestibility of the native protein.
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Chang et al. (1981) studied this question.