Production and characterization of an extensive rapeseed protein hydrolysate

Rapeseed protein isolate has been used as starting material for the generat ion of an extensive protein hydrolysate. Protein hydrolysis was produced by using sequentially an endopeptidase (Alcalase) and an exopeptidase (Flavou rzyme). The final hydrolysate has a 60% degree of hydrolysis and was comple tely soluble between pH values 2.5 and 7. Molecular weight profile of the p rotein hydrolysate was characterized by gel filtration chromatography. A re duction in protein size was observed during the hydrolysis process with acc umulation of small peptides and free amino acids after Flavourzyme digestio n. Amino acid composition of fractions with different molecular weights of the final hydrolysate was analyzed. Some of these fractions, enriched or po or in certain amino acids, could be used for supplementation or treatment o f determined clinical syndromes.