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-F_G) 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-F_G was increased with the increase in the concentration of trypsin. The bitterness of peptides was reduced in LMPC-T-F_G 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.

Among the numerous health benefits of fish consumption, perhaps the most recognized is the role of omega-3 fatty acids in the prevention of cardiovascular disease. Cardiovascular disease is prevalent in Hungary, which has the lowest fish consumption in Europe. Increasing fish consumption is the aim of most European countries and given the high incidence of cardiovascular disease in Hungary, it is of particular importance. A significant reduction of the VAT for fish in 1 January 2018 aimed to increase fish consumption in Hungary. However, despite reduced VAT, the price of fish in Hungary rose from 2017 to 2018. The aim of our research is to explore perceived risks that serve to exacerbate Hungarian consumers’ low fish consumption, and to measure their effects to identify potential strategies to most effectively increase fish consumption. We applied partial least squares structural equation modeling (PLS-SEM) to analyze responses provided by 1042 survey participants (collected with face-to-face interviews, using quota sampling in 2014) to explore variables of fish consumption associated with perceived risk including psychological, physical, social, and functional risks. Our model is the first one that applies detailed perceived risk categories to measure those effects on low fish consumption. The results indicate that psychological risk associated with negative past experiences have both a direct, and through functional risk, an indirect significant negative effect on fish consumption. Conversely, neither social nor physical risk impede Hungarian fish consumption. We conclude that the seafood industry could benefit from targeted interventions that seek to reduce functional risk-perception of the person responsible for preparing fish in the household.

Recently, bioactive peptides as a health-promoting agent have come to the forefront of health research; however, industrial production is limited, possibly due to the lack of the required technological knowledge. The objective of the investigation was to prepare bioactive peptides with hypoallergenic properties from liquid milk protein concentrate (LMPC), through sequential enzymatic and microbial hydrolysis. LMPC was produced from ultra-heat-treated (UHT) skimmed cow’s milk using a nanofiltration membrane. The effect of the concentration of trypsin (0.008–0.032 g·L⁻¹) on the hydrolysis of LMPC was studied. Subsequently, the hydrolysis of tryptic-hydrolyzed LMPC (LMPC-T) with lactic acid bacteria was performed, and the effect of glucose in microbial hydrolysis was studied. Aquaphotomic analysis of the hydrolysis of LMPC was performed using the spectral range of 1300–1600 nm (near-infrared spectra). Changes in antioxidant capacity, anti-angiotensin-converting enzyme activity, and antibacterial activity against Bacillus cereus, Staphylococcus aureus and Listeria monocytogenes were noted after the sequential tryptic and microbial hydrolysis of LMPC. Allergenicity in LMPC was reduced, due to sequential hydrolysis with 0.016 g·L⁻¹ of trypsin and lacteal acid bacteria. According to the aquaphotomic analysis result, there was a dissociation of hydrogen bonds in compounds during the initial period of fermentation and, subsequently, the formation of compounds with hydrogen bonds. The formation of compounds with a hydrogen bond was more noticeable when microbial hydrolysis was performed with glucose. This may support the belief that the results of the present investigation will be useful to scale up the process in the food and biopharmaceutical industries.

Liquid milk protein concentrate with different beneficial values was prepared by membrane filtration and enzymatic modification of proteins in a sequential way. In the first step, milk protein concentrate was produced from ultra-heat-treated skimmed milk by removing milk serum as permeate. A tubular ceramic-made membrane with filtration area 5 × 10⁻³ m² and pore size 5 nm, placed in a cross-flow membrane house, was adopted. Superior operational strategy in filtration process was herein: trans-membrane pressure 3 bar, retention flow rate 100 L·h⁻¹, and implementation of a static turbulence promoter within the tubular membrane. Milk with concentrated proteins from retentate side was treated with the different concentrations of trypsin, ranging from 0.008–0.064 g·L⁻¹ in individual batch-mode operations at temperature 40 °C for 10 min. Subsequently, inactivation of trypsin in reaction was done at a temperature of 70 °C for 30 min of incubation. Antioxidant capacity in enzyme-treated liquid milk protein concentrate was measured with the Ferric reducing ability of plasma assay. The reduction of angiotensin converting enzyme activity by enzyme-treated liquid milk protein concentrate was measured with substrate (Abz-FRK(Dnp)-P) and recombinant angiotensin converting enzyme. The antibacterial activity of enzyme-treated liquid milk protein concentrate towards Bacillus cereus and Staphylococcus aureus was tested. Antioxidant capacity, anti-angiotensin converting enzyme activity, and antibacterial activity were increased with the increase of trypsin concentration in proteolytic reaction. Immune-reactive proteins in enzyme-treated liquid milk protein concentrate were identified with clinically proved milk positive pooled human serum and peroxidase-labelled anti-human Immunoglobulin E. The reduction of allergenicity in milk protein concentrate was enzyme dose-dependent.