Abstract
This paper presents evidence for the occurrence of a trypsin inhibitor in buckwheat grain. Trypsin inhibitor activity distributed uniformly in the whole buckwheat grain. The inhibitor, prepared from aqueous extracts of buckwheat grain by the combined procedures of heat treatment, salting-out and gel filtration, appeared to be a protein-like substance. The inhibitor exhibited significant inhibitory capacity against trypsin and α-chymotrypsin, but less against pepsin, papain, ficin and Nagarse. The inhibitor was relatively thermostable, and highly resistant to acid; susceptibility to pepsin action was so limited to such an extent as to lose about half of its original inhibitory activity. The trypsin inhibitor in buckwheat grain disappeared substantially during germination.
