Sensomics-Assisted Aroma Decoding of Pea Protein Isolates (Pisum sativum L.).

The aroma of pea protein (Pisum sativum L.) was decrypted for knowledge-based flavor optimization of new food products containing pea protein. Sensomics helped to determine several volatiles via ultra-high performance liquid chromatography tandem mass spectrometry and 3-nitrophenylhydrazine derivatization. Among the investigated volatiles, representatives of aldehydes, ketones, and acids were reported in literature as especially important in pea and pea-related matrices. After validation of the method and quantitation of the corresponding analytes, sensory reconstitution as well as omission studies of a selected pea protein were performed and revealed nine odor-active compounds as key food odorants (3-methylbutanal, hexanal, acetaldehyde, (E,E)-2,4-nonadienal, (E)-2-octenal, benzaldehyde, heptanal, 2-methylbutanal, and nonanoic acid). Interestingly, eight out of nine compounds belonged to the chemical class of aldehydes. Statistical heatmap and cluster analysis of all odor activity values of different pea proteins confirmed the obtained sensory results and generalize these nine key food odorants in other pea proteins. The knowledge of key components gained shows potential for simplifying industrial flavor optimization of pea protein-based food.

Quantification of protein-protein interactions in highly denatured whey and potato protein gels.

Understanding the stabilizing protein interactions in protein gels is of high importance for food- and biotechnology. Protein interactions in protein gels can help to predict hardness, deformability and other gel parameters. Currently there are two types methods used. One is to use protein interaction blocking agents and the other is to dissolve the gel in different buffer systems, which cleave the interactions. The first method alters the gelling mechanism, which is why the second method is the preferred one. However, currently published methods are often only suitable for specific gel systems as for example weakly bound protein gels. In this paper, a method is introduced, which is suitable for highly denatured whey and plant protein.•Suitable for strongly cross-linked whey protein and plant protein gels•Stronger buffer system to ensure cleavage of all protein interactions•More reproducible and simplified crushing of the gel without the introduction of uncontrolled shear stress excessively affecting the analysis of chemical bonds.

Sensomics-Assisted Flavor Decoding of Dairy Model Systems and Flavor Reconstitution Experiments.

The whole sensometabolome of a typical dairy milk dessert was decoded to potentially serve as a blueprint for further flavor optimization steps of functional fat-reduced food. By applying the sensomics approach, a wide range of different dairy volatiles, semi and nonvolatiles, were analyzed by ultrahigh-performance liquid chromatography tandem mass spectrometry with or without derivatization presteps. While for volatile sulfur compounds with low odor thresholds, headspace solid-phase microextraction gas chromatography was established, abundant carbohydrates and organic acids were quantified by quantitative 1H nuclear magnetic resonance spectroscopy. Validated quantitation, sensory reconstitution, and omission studies highlighted eight flavor-active compounds, namely, diacetyl, δ-tetra-, δ-hexa-, and δ-octadecalactone, sucrose, galactose, lactic acid, and citric acid as indispensable for flavor recombination. Furthermore, eight odorants (acetaldehyde, acetic acid, butyric acid, methanethiol, phenylacetic acid, dimethyl sulfide, acetoin, and hexanoic acid), all with odor activity values >1, additionally contributed to the overall flavor blueprint. Within this work, a dairy flavor analytical toolbox covering four different high-throughput methods could successfully be established showing potential for industrial applications.