Abstract
Extracts of mature green, dry and germinated Vicia faba beans depressed the trypsin activity of casein. Germination of Vicia faba beans (for 60 h) lowered the trypsin inhibitor (TI) activity. 0.171 M Saline was the most efficient extractant for the TI. Minimal amounts of the TI were extracted in the pH range 4 to 5. The TI of Vicia faba beans was undialysable. The inhibitor activity originated in the seeds at the beginning of pod formation and increased with development of maturity. TI was active only towards trypsin and inactive towards papain, rennin and pepsin. Chromatographing Vicia faba bean proteins, possessing antitryptic activity, on a column of DEAE-cellulose yielded six peaks, all of which possessed antitryptic activity.
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