Chemical and Sensory Evaluation of Umami Taste Derived from Proteolytic Hydrolysate of Pila ampullacea

Abstract

In this study, umami taste was produced and identified from bromelain and trypsin hydrolysate of Pila ampullacea (PA). The PA hydrolysates, obtained from individually bromelain and trypsin with various Enzyme-to-Substrate ratio (E/S) of 1/10, 1/20, and 1/100 (w/v) using divers proteolysis times (3, 6, 9, 12, 15 and 18 h), were evaluated their chemical properties by degree of hydrolysis (DH), total peptide content, and amino acid content. Two chosen proteolysis conditions of PA hydrolysates were concluded by sensory evaluation using hedonic test and principal component analysis (PCA). PA hydrolysate using bromelain with E/S of 1:10 (w/v) for 18 h was one of the 2 chosen proteolysis conditions, which had DH value of 56.56 ± 1.65 %, total peptide content of 10.89 ± 0.09 mg/mL, and amino acid content of 95.34 ± 0.12 ppm. On the other hand, the chosen from trypsin digestion used E/S of 1:10 (w/v) for 15 h, which had DH value of 49.71 ± 0.22 %, total peptide content of 6.44 ± 0.28 mg/mL, and amino acid content of 81.43 ± 1.29 ppm. PA hydrolysates were subjected to explain the released peptides using liquid chromatography-tandem mass spectrometry (LC-MS/MS) and database-assisted identification. There were many identified peptides contained in PA hydrolysates that contributed to umami taste. Their sequences from bromelain digestion were GPEGPQGPPGPRG, GIMLGAA, GLPGLPGLKGDPGEPGLP, GKDGEAG, GLVMDSCAGH, and EEKITEDDDAVGDDAENR. Several peptide fragments from trypsin digestion were GQTVIGL, GLPGLPGLSGPKG, DTGPAGPAGPAGPQGPR and QTLEKALSHVIQEFETEKQLITVNAR.