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The bitterness in soy protein hydrolysates is a major obstacle to acceptance of soy products by consumers. The primary objective of this research was to evaluate the bitterness of 4 different molecular weight peptide fractions obtained from Protex 7L-treated soy hydrolysate. First, a theoretical analysis was performed to predict hydrolytic cleavage points of 3 different bitterand non-bitter-producing proteases on soy protein at 4% degree of hydrolysis (DH) and hypothesize how peptide size influences bitterness. Protex 7L-treated soy hydrolysate was fractionated by gel filtration, desalinated by ultra-filtration, freezedried, and re-diluted to 5% w/v in Milli-Q water for sensory evaluation. Molecular weight of the fractions was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Panelists’ sensitivity to Multifect Neutral (MN)-treated soy hydrolysate was compared to caffeine, quinine, leucine, and phenylalanine. Panelists’ perceptions of the bitterness of MN-treated soy hydrolysate were compared to the bitterness of leucine and phenylalanine free amino acids. Panelists were screened for bitterness sensitivity and 15 highly sensitive panelists were selected to evaluate the Protex 7L-treated soy hydrolysate fractions, MN-treated soy hydrolysate, caffeine, quinine, leucine, and phenylalanine by using a modified triangle test. Comparison of panelist sensitivity was evaluated by Cohen's kappa coefficient and Fisher’s exact test (p ≤ 0.05). Comparison of bitterness was analyzed by Cohen's kappa coefficient and McNemar’s test (p ≤ 0.05). A fraction consisting of low molecular weight peptides (estimated 1-5 kDa) was identified as bitter (p = 0.009) as well as the unfractionated hydrolysate (p = 0.088). The remaining 3 fractions (2 larger MW and one < 1 kDa) were not bitter. Panelists selected for bitterness sensitivity had an average threshold of 0.98 mM for caffeine, 8.9 μM for quinine,

Bitterness of soy protein hydrolysates according to molecular weight of peptides