Detecting the Bitterness of Milk-Protein-Derived Peptides Using an Electronic Tongue

Abstract

Bitterness is a considerable limiting factor for the application of bioactive peptides in the food industry. The objective of this study was to compare the level of bitterness of milk-protein-derived peptides using an electronic tongue (E-tongue). Liquid milk protein concentrate (LMPC) was prepared from ultra-heat-treated skimmed cow’s milk. It was initially hydrolyzed with different concentrations of trypsin, namely, 0.008 g·L−1, 0.016 g·L−1 and 0.032 g·L−1. In a later exercise, tryptic-hydrolyzed LMPC (LMPC-T) was further hydrolyzed using Lactobacillus bulgaricus and Streptococcus thermophilus. The effect of glucose in microbial hydrolysis was studied. The bitterness of peptides was evaluated with respect to quinine, a standard bittering agent. The level of bitterness of the peptides after microbial hydrolysis of LMPC-T (LMPC-T-F and LMPC-T-FG) was evaluated using a potentiometric E-tongue equipped with a sensor array that had seven chemically modified field-effect transistor sensors. The results of the measurements were evaluated using principal component analysis (PCA), and subsequently, a classification of the models was built using the linear discriminant analysis (LDA) method. The bitterness of peptides in LMPC-T-F and LMPC-T-FG was increased with the increase in the concentration of trypsin. The bitterness of peptides was reduced in LMPC-T-FG compared with LMPC-T-F. The potential application of the E-tongue using a standard model solution with quinine was shown to follow the bitterness of peptides.

Keywords

• milk-protein-derived peptides
• enzymatic hydrolysis
• microbial hydrolysis
• bitterness
• electronic tongue
• correlative analysis of bitterness