Search

This work studies the emulsifying and antioxidant properties of potato protein hydrolysates (PPHs) fractions obtained through enzymatic hydrolysis of potato protein using trypsin followed by ultrafiltration. Unfractionated (PPH1) and fractionated (PPH2 as >10 kDa, PPH3 as 10-5 kDa, PPH4 as 5-0.8 kDa, and PPH5 as 10 kDa showed the highest ability to decrease oil-water interfacial tension. All PPH fractions predominantly provided elastic, weak, and easily stretchable interfaces. PPH2 provided a more rigid interfacial layer than the other hydrolysates. Radical scavenging and metal chelating activities of PPHs were also tested and the highest activities were provided by the unfractionated hydrolysate and the fractions with peptides >5 kDa. Furthermore, the ability of PPHs to form physically and oxidatively stable 5% fish oil-in-water emulsions (pH 7) was investigated during 8-day storage at 20 °C. Our results generally show that the fractions with peptides >5 kDa provided the highest physicochemical stability, followed by the fraction with peptides between 5 and 0.8 kDa. Lastly, promising sensory results with mostly mild attributes were obtained even at protein concentration levels that are higher than needed to obtain functional properties. The more prominent attributes (e.g., bitterness and astringency) were within an acceptable range for PPH3 and PPH4.

Peptides and protein hydrolysates are promising alternatives to substitute chemical additives as functional food ingredients. In this study, we present a novel workflow for producing a potato protein hydrolysate with improved emulsifying and foaming properties using quantitative proteomics and bioinformatic prediction to facilitate targeted hydrolysis design. Based on previous studies, we selected 15 potent emulsifier peptides derived from abundant potato proteins as targets. Through in silico analysis, we determined that from a range of industrial proteases (Neutrase (Neut), Alcalase (Alc), Flavourzyme (Flav) and Trypsin (Tryp)), Tryp was found more likely to release peptides resembling the targets. After applying all proteases individually, hydrolysates were assayed for in vitro emulsifying and foaming properties. No direct correlation between degree of hydrolysis and interfacial properties was found. Tryp (E/S = 3%) produced a hydrolysate (DH = 5.4%) with high aqueous solubility and the highest (P < 0.05) emulsifying and foaming abilities, validating the hypothesis. Using LC-MS/MS, we identified >10,000 peptides in each hydrolysate. Peptide mapping revealed that random overlapping with known peptide emulsifiers is not sufficient to quantitatively describe hydrolysate functionality. However, validated release of targeted peptides by 3% Tryp appears to increase surface activity of the hydrolysate. Our data also suggest that terminal hydrophobic anchor domains may be important for high interfacial partitioning and activity. While modest yields and residual unhydrolyzed protein indicate room for process improvement, this work shows that bioinformatics-guided and data-driven targeted hydrolysis is a promising, interdisciplinary approach to facilitate process design for production of functional hydrolysates from alternative protein sources.

Peptides and protein hydrolysates are promising alternatives to substitute chemical additives as functional food ingredients. In this study, we present a novel approach for producing a potato protein hydrolysate with improved emulsifying and foaming properties by data-driven, targeted hydrolysis. Based on previous studies, we selected 15 emulsifier peptides derived from abundant potato proteins, which were clustered based on sequence identity. Through in silico analysis, we determined that from a range of industrial proteases (Neutrase (Neut), Alcalase (Alc), Flavorzyme (Flav) and Trypsin (Tryp)), Tryp was found more likely to release peptides resembling the target peptides. After applying all proteases individually, hydrolysates were assayed for in vitro emulsifying and foaming properties. No direct correlation between degree of hydrolysis and interfacial properties was found. Tryp produced a hydrolysate (DH=5.4%) with the highest (P10,000 peptides in each hydrolysate. Through peptide mapping, we show that random overlapping with known peptide emulsifiers is not sufficient to quantitatively describe hydrolysate functionality. While Neut hydrolysates had the highest proportion of peptides with target overlap, they showed inferior interfacial activity. In contrast, Tryp was able to release specifically targeted peptides, explaining the high surface activity observed. While modest yields and residual unhydrolyzed protein indicate room for process improvement, this work shows that data-driven, targeted hydrolysis is a viable, interdisciplinary approach to facilitate hydrolysis design for production of functional hydrolysates from alternative protein sources.

Aquesta publicació s'elabora a partir de les contribucions de cadascú dels membres nacionals que integren la Network of Eufound Correspondent. Pel cas d'Espanya la contribució ha estat realitzada per l'Alejandro Godino, Digital transformation is changing the world of work. This report looks at how social partners - the actors involved in the regulation of employment relationships - are increasingly adopting technological solutions to improve the services that they provide to their members and facilitate collective bargaining processes. Technological tools offer social partners the opportunity to enhance consultation, engage with their members through digitised processes, improve services and increase networking activities, as well as addressing the issue of membership decline. The findings of this report show that the extent to which the social partners use digital technologies varies greatly across the EU Member States, Norway and the United Kingdom. Provisions in collective agreements on several aspects of digitalisation have been identified in about half of the countries. Through these provisions, social partners encourage their members to boost training on digital skills, ensure fair and safe working conditions and take account of data protection and employee monitoring practices. The European social partners' autonomous framework agreement on digitalisation has provided inspiration to national-level organisations, and follow-up actions in this regard have the potential to greatly benefit their members.