The susceptibility of crystalline and amorphous proteins from beans to enzymatic hydrolysis were compared. The crystalline proteins were obtained by precipitating the crystals (5°C, 18 h) from acid extracts. The amorphous forms were obtained by isoelectric precipitation of proteins from alkaline extracts. The content of proteins in crystalline forms was higher (81-82%) than in amorphous forms (77%). The differences were observed for the susceptibilities of crystalline and amorphous proteins to enzymes. The crystalline proteins showed higher values for in vitro digestibility (80-81%) than amorphous proteins (78-80%). The reverse relationship was observed when the proteins were digested with one enzyme, i.e. trypsin, and the results were monitored by electrophoretical separation of proteins and by determining the increase in free a-amino groups.
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