Abstract:

Bioactive proteins were recovered from a liquid byproduct containing roughly 1.5% protein, with approximately 50%
being protease inhibitors by expanded bed adsorption using macroporous resin Amberlite XAD7HP. The recovered proteins were
analyzed for amino acid composition. The results indicated that XAD7HP allowed the separation between protease inhibitors and
patatin. The protease inhibitors exhibited an activity of 410 mg/g against trypsin and contained Ser, Leu and Glu at 3.2, 9.14 and
8.14 g/100 g, respectively, with the ratio of essential to total amino acids being 40.80%. Similarly, hydrophobic amino acids, Ile,
Leu, Val, Phe and Tyr, were present in relatively higher quantities in these protease inhibitors.

Key words: potato, native protein, protease inhibitor, amino acid composition