Formation of Digestion Intermediate of Glycinin

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Abstract
The kinetics of the tryptic proteolysis of glycinin were studied by the pH-stat method. The results clearly indicated the existence of at least two simultaneous reactions proceeding at different rates. The rate constants suggested that a group of peptide bonds was much more susceptible to proteolytic attack than others. In addition stable digestion intermediates were expected in the degradation course. In a low ionic strength condition, 3 or 4 electrophoretic bands were formed, whereas only single band was seen in high ionic strength buffer. The major intermediate in a high ionic strength condition (glycinin-T) was isolated by Sepharose 6B chromatography. Glycinin-T showed a single band on polyacrylamide gel electrophoresis. Acidic subunits of glycinin were digested forming 13,500 and 16,000 molecular weight fragments, whereas basic subunits were not digested at all.

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