Digestibility and Proteinase Inhibitory Action of a Kidney Bean Globulin
نویسندگان
چکیده
A globulin fraction, isolated from black beans (Phaseolus vulgaris), was resistant to hydrolysis by pepsin, trypsin, chymotrypsin, papain, ficin, hurain, and subtilisin. After denaturation of the globulin by heat or urea, only slight hydrolysis by enzymes could be detected. The activity of all seven proteinases on their respective substrates was inhibited by the bean globulin. Preincubation of enzyme and globulin enhanced the inhibitory effect. When heat denatured, insoluble globulin was stirred with papain, proteolytic activity was diminished.
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