Lentil meal proteins were treated by chymotrypsin. Hydrolysis was controlled with the pH-stat method. Degree of hydrolysis (DH) was evaluated and after 120 min of the process amounted to 13%. SDS-PAGE and SE-HPLC methods were used to study molecular weight distribution of lentil meal proteins and their chymotryptic hydrolysates of DH 2%, 4%, 8% and 12 %. Bands in the range of 21–66 kDa were predominant on the electrophoregram of lentil proteins. Chymotrypsin treatment resulted in releasing the hydrolysis products of both high molecular weight (62,000; 30,500 Da) molecules and small peptides (<6,500 Da). At the first stage of hydrolysis (DH 2.0%) intermediate products are formed, which are then further hydrolysed. Chromatographic separation confirmed the results of SDS-PAGE. Larger polypeptides and unhydrolysed proteins are present in hydrolysate of DH 12% but products of hydrolysis with molecular weight of 0.5–6.5 kDa are predominant. No simple correlation between degree of hydrolysis and intensity of bitterness and astringency sensation was noticed. Bitterness of hydrolysates was not high (2.25-2.35 a.u.).