Biochemical characteristics of trypsin inhibitor from wheat grain, beta variety.

A homogenous trypsin inhibitor from wheat grain has been characterized. It is a protein of molecular weight 9105 Da and isoelectric point pI = 9.5.

Some biochemical properties of trypsin inhibitor type antinutrients derived from extracts of wheat grain, Beta variety.

Trypsin inhibitors were isolated and partially purified from wheat grain, Beta variety. The procedure for determination of the inhibitory activity was simplified. This pertains shortening of the reaction time as well as quantitative decrease of components in the incubation mixture.

Plant inhibitors of proteolytic enzymes.

The presence of inhibitors of proteinases was stated in many species of plants. There are macropeptides of the molecular weight ranging from 3700 to 8000, often bound to carbohydrates. Potential sources of inhibitors of proteinases are legumes, cereals, potatoes and also some fruits.