The present study identifies the adulteration of walnut products by other edible nuts, specifically cashew, hazelnut, and peanut by bottom-up proteome analysis. The protein extracts of the samples were proteolytically digested and analyzed by micro-flow liquid chromatography ion mobility quadrupole time-of-flight mass spectrometry (microLC-IM-QTOF) with subsequent peptide profiling. Guided peptide identification in the non-target LC-MS/MS data was optimized using a custom protein sequence database, leading to the identification of 11 selective marker peptides for the examined matrices cashew, hazelnut, and peanut. Adulteration levels down to 1% (w/w) could be reliably detected in spiked walnut samples. The authenticity of an independent test set with eight potentially adulterated samples was assessed in comparison to 27 authentic reference samples, achieving 100% accuracy. The acquired non-targeted LC-MS/MS data allow post-hoc re-processing with different protein sequence databases, in case other adulterants should be investigated.

The effects of novel wall materials for Chlorella vulgaris were reported using spray-drying in our previous study. In this study, we extend this work by applying freeze-drying, another major and widely used encapsulation technique, and encapsulate C. vulgaris biomass using this method. The experimental design was prepared using the Simplex-Lattice Mixture Design method. The independent variables were combinations of various wall materials such as maltodextrin (18-20 DE), inulin (DP < 10), aquafaba, and deactivated yeast as spray-dried Saccharomyces cerevisiae cells (25.0%-75.0%, w/w, in dm) and C. vulgaris biomass (25.00%-100.0%, w/w, in dm). The amounts of pigments, crude protein, physicochemical and color properties, wettability, hygroscopicity, and drying and encapsulation efficiency of the samples were determined. Significant models (p < 0.05) for moisture (1.30-3.36 g/100 g), total carotenoid (0.36-1.62 mg/g), total chlorophylls (8.51-29.8 mg/g), and crude protein (6.40-43.8 g/100 g) contents were obtained. Furthermore, it was found that the size and coalescence trends of the samples were influenced by the maltodextrin ratio used. Based on the results of this study, innovative materials such as deactivated yeast and aquafaba have significant potential for use in microalgae encapsulation and drying.

ABSTRACT The present study analyzed the impact of Streptococcus thermophilus (ST), Lactobacillus delbrueckii subsp. bulgaricus (LB), and endogenous milk enzymes on protein hydrolysis during early‐stage lactic acid fermentation of milk. Untargeted peptide profiling of milk fermented with single or mixed cultures of ST and LB and unfermented controls was applied covering peptides between 4 and 45 amino acids. Thus, more than 3000 peptides were identified. LB in single and mixed culture led to the highest proteolytic activity (up to 50% higher than controls), the highest number of peptides [1270 unique peptides vs. 124 (ST) and 439 (controls)], and the highest number of bioactive peptides [109 vs. 37 (ST) and 79 (controls)]. Shorter peptides (4–15 amino acids) were predominantly hydrolyzed by ST and generated by LB. Distinct cleavage sites that were detected in all samples could be attributed to milk enzymes like plasmin. Proteolysis by bacterial enzymes showed low specificity.

Milk processing can reduce protein quality mainly by lactosylation. For quality control, global protein lactosylation can be determined by HPLC-DAD via furosine, formed during acid hydrolysis. Alternatively, lactulosyllysine can be directly measured by site-specific relative quantitation using UHPLC-ESI-MS/MS-sMRM. The study aimed to compare global furosine analysis with analysis of lactulosyllysine at K8, K14, K47, K60, K69/70, K75/77/83, K91, K100/101, and K135 of β-lactoglobulin to evaluate lactosylation. A linear positive correlation between the modification indices of all analyzed lysine residues and the furosine content in raw milk samples heated for 0, 3, 6, 9, 12, and 15 min at 120 °C was detected (r = 0.9763-0.9921). In commercial milk products (pasteurized milk, ESL milk, UHT milk, sterilized milk, condensed milk, and coffee cream), both methods reflected the different heat loads during production. The furosine value detected slight differences more selectively, whereas UHPLC-ESI-MS/MS-sMRM revealed some site-specific effects.

ABSTRACTThe present study aimed to identify antioxidative and angiotensin converting enzyme (ACE) inhibitory peptides in fermented buttermilk after simulated gastric digestion. Following isoelectric focusing fractionation, peptides of the most active fractions were identified by ultrahigh performance liquid chromatography–tandem mass spectrometry (UHPLC–MS/MS). Subsequently, 23 peptides were synthesized and tested for antioxidative and ACE inhibitory activity. The peptide PR7 (PWDQVKR, αs2‐casein 108–114) exerted comparable antioxidative activity to ascorbic acid, whereas the peptide SF8 (SGPLRPFF, butyrophilin 427–434) efficiently inhibited ACE with an IC50 value of 1.57 µM. The binding modes of the five most active ACE inhibitors were predicted using AlphaFold2 multimer software. Molecular mechanics (MM) minimization and molecular dynamics (MD) simulations of all complexes, followed by MM‐generalized born surface area (GBSA) binding energy calculations, were predicted. Notably, these peptides manifested good binding affinities to ACE. The estimated MM‐GBSA/MD binding energies correlated with the detected IC50 values [correlation coefficient (R2) = 0.79]. Post‐MD analyses over 100 ns elucidated the steadiness of the five peptides.

We explored changes in the peptide profiles of pasteurized milk during its shelf life. Our hypothesis was that residual enzymatic activity after pasteurization would systematically alter the peptide profile, enabling the identification of single peptides as markers for proteolysis. Two independent storage experiments were conducted, and the peptide profiles were recorded with microLC-QTOF MS/MS. The first experiment resulted in the identification of 2464 peptides. During the ten-day storage, 30 peptides showed significant changes. The second experiment involved four samples that were analyzed at the beginning, middle, and end of their shelf lives. Combining the results of both experiments revealed that seven key peptides were strongly associated with storage. Five of these peptides were derived from β-casein, indicating its susceptibility to proteolysis by endogenous and microbial proteases. These findings confirm that single peptides reflect storage-related changes and could serve as markers for product stability, quality control, and storage optimization strategies.

Ripened cheeses contain bioactive peptides that are released from caseins by enzymatic hydrolysis during fermentation and ripening. However, the physiological relevance of these peptides depends on their stability during gastrointestinal digestion and their bioavailability. This study aimed to assess the impact of digestion on the peptide profile of the young Gouda Holland cheese. Using liquid chromatography coupled to electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS), we monitored the peptide profile changes during in vitro simulated gastrointestinal digestion. In total, 54 peptide sequences were identified in cheese (20), gastric (20), and intestinal digests (24). Ten peptides were derived from αs1-casein, 43 from β-casein, and 1 from κ-casein. Most of the identified peptides were exclusive to one of the analyzed samples, revealing the alteration of the peptide profile during digestion. Two peptides were resistant to digestion, including β-CN(f193-209) with reported antithrombin, antimicrobial, and ACE-inhibitory effects. These results demonstrate the dual role of digestion in both degrading and releasing bioactive peptides and emphasize the importance of using digestion models to assess the bioactive potential of peptides in dairy products.

For cleaner and sustainable production, industrial food waste reuse studies are great of importance. In this study, to develop a novel bulking agent from the liquid wastes of colorant production processes obtained from red beet extract (RBW), an optimization study with an 18-point experimental point was performed in a pilot spray dryer by using maltodextrin as a carrier material for drying. The spray drying inlet temperature (120-140 degrees C) and the ratios of carrier agent (10%-25%) and liquid waste (75%-90%) in the feed solution were independent variables. Optimization responses were drying yield (44.4-86.6%) and moisture content (1.39-3.89 g/100 g). In addition, physicochemical (water activity, color, pH), particle size distribution, and various powder characteristics of the samples were investigated. Significant models for responses were determined (P < 0.05). The optimum conditions (Desirability: 0.876) for RBW drying were determined and validated as 120 degrees C spray dryer inlet temperature, and feed solution containing 90% RBW and 10% maltodextrin in dry matter. As a result, powders obtained from RBW have the potential to be used as a bulking agent in food formulations due to their composition and low moisture content, water activity and drying yield (>80.0%). According to our results, it may be possible to prevent the release of RBW which has high COD and BOD values and to decrease the production and waste treatment costs of the colorant industry. However, the limitations of the novel bulking agent as residual pigments and total ash content should be considered for further food applications.

The present study aimed to identify endogenous milk peptides for species differentiation independent of heat exposure. Thus, comprehensive milk peptide profiles from five species and three types of heat treatments were analyzed by micro-flow liquid chromatography ion mobility quadrupole time-of-flight mass spectrometry (microLC-IM-QTOF) with subsequent database search leading to >= 3000 identified peptides. In the milks, 1154 peptides were unique for cow, 712 for sheep, 466 for goat, 197 for buffalo, and 69 for mare. Most peptides were detected in extended-shelf life (ESL) milk (2010), followed by ultra-high temperature (UHT) processed (1474) and pasteurized milk (1459 peptides), with 693 peptides present in all milk types. A blind test set of 64 samples confirmed eight species-specific, but heat-independent marker peptides in milk from cow, seven from goat, six from sheep, nine from buffalo, and three from mare. The generated peptide profiles can also be used to identify species- and heat-specific markers.

In this study, the effects of gelatin concentrations (GC) (5.0-10.0 g/100 g), mixing rate (MR) (100-1100 rpm), and gelatin addition temperature (GAT) (55, 60, and 65°C) were investigated on the main textural and various physicochemical properties of model gels (n = 72) prepared using sucrose and glucose syrup (40-42 DE). Considering the p-value of the F-statistic calculated by analysis of variance and the 5% significance level, the production parameters and their interactions had a significant effect on the quality parameters. The influence of the production parameters GC, MR, and GAT, and the interaction of these parameters, GC * MR, GC * GAT, MR * GAT, and GC * MR * GAT of the model gels on the quality characteristic were expressed by converting the Type III SS values into percent values. When all quality characteristics were considered together, MR was the most influential with a score of 58%. PCAmix, a combination of factorial analysis with PCA, was used to visualize the correlations between the production parameters and the quality characteristics of the modeled gels. A great influence was observed between MR and moisture content, color properties, and texture parameters, except springiness. A moderate effect of GC and a minor effect of GAT could be characterized. With the 2D-map of observations, the model gels could be clearly divided into two groups according to the MRs. In accordance with the observations diagram of PCAmix, the similarity dendrogram of AHC also formed two clusters, one cluster for the samples with MR 100 and 200 rpm and one cluster for the samples with MR 500 and 1100 rpm.

The influence of data evaluation parameters on qualitative and quantitative results of untargeted shotgun profiling of enzymatic and nonenzymatic post-translational modifications (PTMs) was investigated in a model of bovine whey protein α-lactalbumin heated with lactose. Based on the same raw data, individual adjustments to the protein database and enzyme settings of PEAKS studio software increased the identification rate from 27 unmodified peptides to 48 and from 322 peptides in total to 535. The qualitative and quantitative reproducibility was also assessed based on 18 measurements of one sample across three batches. A total of 570 peptides were detected. While 89 peptides were identified in all measurements, the majority of peptides (161) were detected only once and mostly based on nonindicative spectra. The reproducibility of label-free quantification (LFQ) in six measurements of the same sample was similar after processing the data by either the PTM algorithm or the LFQ algorithm. In both cases, about one-third of the peptides showed a coefficient of variation of above 20%. However, the LFQ algorithm increased the number of quantified peptides from 75 to 179. Data are available at the PRIDE Archive with the data set identifier PXD050363.

In this study, we discussed covalent and non-covalent reactions between cocoa polyphenols and proteins (milk and cocoa) and the possible effects of these reactions on their bioaccessibility, considering environmental and processing conditions. Better insight into these interactions is crucial for understanding the biological effects of polyphenols, developing nutritional strategies, and improving food processing and storage. Protein-polyphenol reactions affect the properties of the final product and can lead to the formation of various precursors at various stages in the manufacturing process, such as fermentation, roasting, alkalization, and conching. Due to the complex composition of the chocolate and the various technological processes, comprehensive food profiling strategies should be applied to analyze protein-polyphenol covalent reactions covering a wide range of potential reaction products. This will help to identify potential effects on the bioaccessibility of bioactive compounds such as low-molecular-weight peptides and polyphenols. To achieve this, databases of potential reaction products and their binding sites can be generated, and the effects of various process conditions on related parameters can be investigated. This would then allow to a deeper insight into mechanisms behind protein-polyphenol interactions in chocolate, and develop strategies to optimize chocolate production for improved nutritional and sensory properties.

LebensmittelchemieVolume 78, Issue S1 p. S1-026-S1-026 Abstract Freisetzung von Peptiden aus Milchproteinen durch die Joghurtstarterkulturen S. thermophilus und Lb. bulgaricus Eva Beck, Eva Beck Lehrstuhl für Lebensmittelchemie, Department Chemie und Pharmazie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorLena Riedinger, Lena Riedinger Lehrstuhl für Lebensmittelchemie, Department Chemie und Pharmazie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorSevim Dalabasmaz, Sevim Dalabasmaz Lehrstuhl für Lebensmittelchemie, Department Chemie und Pharmazie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorRohtraud Pichner, Rohtraud Pichner Fachbereich Oecotrophologie, Hochschule Fulda, Leipziger Str. 123, 36037 FuldaSearch for more papers by this authorMonika Pischetsrieder, Corresponding Author Monika Pischetsrieder [email protected] Lehrstuhl für Lebensmittelchemie, Department Chemie und Pharmazie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, 91058 Erlangen[email protected]Search for more papers by this author Eva Beck, Eva Beck Lehrstuhl für Lebensmittelchemie, Department Chemie und Pharmazie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorLena Riedinger, Lena Riedinger Lehrstuhl für Lebensmittelchemie, Department Chemie und Pharmazie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorSevim Dalabasmaz, Sevim Dalabasmaz Lehrstuhl für Lebensmittelchemie, Department Chemie und Pharmazie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorRohtraud Pichner, Rohtraud Pichner Fachbereich Oecotrophologie, Hochschule Fulda, Leipziger Str. 123, 36037 FuldaSearch for more papers by this authorMonika Pischetsrieder, Corresponding Author Monika Pischetsrieder [email protected] Lehrstuhl für Lebensmittelchemie, Department Chemie und Pharmazie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, 91058 Erlangen[email protected]Search for more papers by this author First published: 01 March 2024 https://doi.org/10.1002/lemi.202452016AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat No abstract is available for this article. References 1A. Zourari et al., Le Lait, 1992 72 (1), 1-34. 10.1051/lait:199211 Google Scholar 2Rodriguez-Serrano G. M. et al., J Microbiol Biotechnol, 2018 28 (10), 1581-1588. 10.4014/jmb.1807.07017 CASPubMedWeb of Science®Google Scholar Volume78, IssueS1Supplement: Abstracts der Vorträge der Regionalverbände und die der Posterflashtalks der AG JLCMarch/April 2024Pages S1-026-S1-026 ReferencesRelatedInformation

Sheep farming is an important socioeconomic activity in most Mediterranean countries, particularly Spain, where it contributes added value to rural areas. Sheep milk is used in Spain mainly for making cheese, but it can be used also for making other dairy products, such as the lactic-alcoholic fermentation product known as kefir. Dairy products have health benefits because, among other reasons, they contain molecules with biological activity. In this work, we performed a proteomics strategy to identify the peptidome, i.e., the set of peptides contained in sheep milk kefir fermented for four different periods of time, aiming to understand changes in the pattern of digestion of milk proteins, as well as to identify potential bioactive peptides. In total, we identified 1942 peptides coming from 11 different proteins, and found that the unique peptides differed qualitatively among samples and their numbers increased along the fermentation time. These changes were supported by the increase in ethanol, lactic acid, and D-galactose concentrations, as well as proteolytic activity, as the fermentation progressed. By searching in databases, we found that 78 of the identified peptides, all belonging to caseins, had potential biological activity. Of these, 62 were not previously found in any milk kefir from other animal species. This is the first peptidomic study of sheep milk kefir comprising time-course comparison.

LebensmittelchemieVolume 77, Issue S3 p. S3-124-S3-124 Analytik Enzyme mapping to elucidate the role of endogenous proteolytic enzymes on the native peptide profile of bovine milk L. Riedinger, L. Riedinger Erlangen/DSearch for more papers by this authorA. Mauser, A. Mauser Erlangen/DSearch for more papers by this authorT. M. Schichtl, T. M. Schichtl Erlangen/DSearch for more papers by this authorDr. S. Dalabasmaz, Dr. S. Dalabasmaz Erlangen/D Lehrstuhl für Lebensmittelchemie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, Erlangen/DSearch for more papers by this author L. Riedinger, L. Riedinger Erlangen/DSearch for more papers by this authorA. Mauser, A. Mauser Erlangen/DSearch for more papers by this authorT. M. Schichtl, T. M. Schichtl Erlangen/DSearch for more papers by this authorDr. S. Dalabasmaz, Dr. S. Dalabasmaz Erlangen/D Lehrstuhl für Lebensmittelchemie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, Erlangen/DSearch for more papers by this author First published: 01 August 2023 https://doi.org/10.1002/lemi.202359105AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat No abstract is available for this article. References [1]P. F. Fox, P. L. H. McSweeney, Dairy Chemistry and Biochemistry 1998, 146–237. [2]P. F. Fox, Encyclopedia of Dairy Science 2002, 1805–1812. [3]A. L. Kelly et al, Int. Dairy Journal 2006, 16, 563–572. [4]H. C. Deeth, M. J. Lewis, High Temperature Processing of Milk and Milk Products 2017. [5]H. C. Deeth, M. J. Lewis, in Milk Processing and Quality Management 2009, 168–209. Volume77, IssueS3Supplement: Abstracts der Vorträge, Posterflashtalks und Poster von den 51. Deutschen Lebensmittelchemietagen 2023August 2023Pages S3-124-S3-124 ReferencesRelatedInformation

LebensmittelchemieVolume 77, Issue S3 p. S3-073-S3-073 Analytik Development of an untargeted proteomics-based strategy for monitoring polyphenol-protein reactions: A model study with (-)-epicatechin and ß-lactoglobulin. A. Börsig, A. Börsig Erlangen, Braunschweig/DSearch for more papers by this authorN. Konar, N. Konar Ankara/TRSearch for more papers by this authorDr. S. Dalabasmaz, Dr. S. Dalabasmaz Erlangen/D Sevim Dalabasmaz, Lehrstuhl für Lebensmittelchemie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, 91058 Erlangen, DSearch for more papers by this author A. Börsig, A. Börsig Erlangen, Braunschweig/DSearch for more papers by this authorN. Konar, N. Konar Ankara/TRSearch for more papers by this authorDr. S. Dalabasmaz, Dr. S. Dalabasmaz Erlangen/D Sevim Dalabasmaz, Lehrstuhl für Lebensmittelchemie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, 91058 Erlangen, DSearch for more papers by this author First published: 01 August 2023 https://doi.org/10.1002/lemi.202359054AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat No abstract is available for this article. References [1]H.-D. Belitz, W. Grosch, P. Schieberle, Food chemistry. 2004, 939–969. [2]M.A. Martin, S. Ramos, Food Chem. Toxicol. 2021, 151, 112121. [3]S. Rohn, Food Res. Int 2014, 65, 13–19. [4]S. Dalabasmaz et al., Crit. Rev. Food. Sci. Nutr. 2023, 1–13. [5]A. Börsig, N. Konar, S. Dalabasmaz, Food Chemistry. 2023, 408, 135242. Volume77, IssueS3Supplement: Abstracts der Vorträge, Posterflashtalks und Poster von den 51. Deutschen Lebensmittelchemietagen 2023August 2023Pages S3-073-S3-073 ReferencesRelatedInformation

Bioactive peptides, released from buttermilk by fermentation and/or gastrointestinal proteases, may have health promoting effects. Thus, a comprehensive analysis of the peptide fraction of fermented buttermilk, before and after different phases of simulated gastrointestinal digestion, was performed using ultra high-performance liquid chromatography-electrospray ionization-tandem mass spectrometry (UHPLC-ESI-MS/MS). Results showed that digestion simulation substantially changed the peptide profile of fermented buttermilk. A total of 81, 120 and 46 peptides were identified in fermented buttermilk, its gastric and intestinal digests, respectively. These peptides released mostly from β-casein followed by αs1-casein, κ-casein and β-lactoglobulin. In addition, 14 peptides released from milk fat globule membrane proteins (lactadherin, butyrophilin and GlyCAM-1). Bioactivity, mainly angiotensin converting enzyme (ACE) inhibitory activity, has been reported before for only 54 of the detected peptides. Radical scavenging, ferric reducing and ACE inhibitory activities of fermented buttermilk peptides increased significantly after digestion, indicating promotion in fermented buttermilk-peptide bioactivity by gastrointestinal digestion.

LebensmittelchemieVolume 77, Issue S3 p. S3-067-S3-067 Analytik Analyse des Peptidprofils von mit S. thermophilus und Lb. Bulgaricus fermentierter pasteurisierter Milch mittels mikroLC-IM-QTOF-MS/MS E. Beck, E. Beck Erlangen/D Friedrich-Alexander-Universität Erlangen-Nürnberg, Lehrstuhl für Lebensmittelchemie, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorN. Zenk, N. Zenk Erlangen/D Friedrich-Alexander-Universität Erlangen-Nürnberg, Lehrstuhl für Lebensmittelchemie, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorJ. Stützer, J. Stützer Erlangen/D Friedrich-Alexander-Universität Erlangen-Nürnberg, Lehrstuhl für Lebensmittelchemie, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorL. Bähr, L. Bähr Erlangen/D Friedrich-Alexander-Universität Erlangen-Nürnberg, Lehrstuhl für Lebensmittelchemie, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorS. Dalabasmaz, S. Dalabasmaz Erlangen/D Friedrich-Alexander-Universität Erlangen-Nürnberg, Lehrstuhl für Lebensmittelchemie, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorR. Pichner, R. Pichner Fulda/D Friedrich-Alexander-Universität Erlangen-Nürnberg, Lehrstuhl für Lebensmittelchemie, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorM. Pischetsrieder, M. Pischetsrieder Erlangen/D Friedrich-Alexander-Universität Erlangen-Nürnberg, Lehrstuhl für Lebensmittelchemie, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this author E. Beck, E. Beck Erlangen/D Friedrich-Alexander-Universität Erlangen-Nürnberg, Lehrstuhl für Lebensmittelchemie, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorN. Zenk, N. Zenk Erlangen/D Friedrich-Alexander-Universität Erlangen-Nürnberg, Lehrstuhl für Lebensmittelchemie, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorJ. Stützer, J. Stützer Erlangen/D Friedrich-Alexander-Universität Erlangen-Nürnberg, Lehrstuhl für Lebensmittelchemie, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorL. Bähr, L. Bähr Erlangen/D Friedrich-Alexander-Universität Erlangen-Nürnberg, Lehrstuhl für Lebensmittelchemie, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorS. Dalabasmaz, S. Dalabasmaz Erlangen/D Friedrich-Alexander-Universität Erlangen-Nürnberg, Lehrstuhl für Lebensmittelchemie, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorR. Pichner, R. Pichner Fulda/D Friedrich-Alexander-Universität Erlangen-Nürnberg, Lehrstuhl für Lebensmittelchemie, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this authorM. Pischetsrieder, M. Pischetsrieder Erlangen/D Friedrich-Alexander-Universität Erlangen-Nürnberg, Lehrstuhl für Lebensmittelchemie, Nikolaus-Fiebiger-Str. 10, 91058 ErlangenSearch for more papers by this author First published: 01 August 2023 https://doi.org/10.1002/lemi.202359048AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat No abstract is available for this article. Literatur [1]A. Zourari et al., Le Lait, 1992, 72 (1), 1–34. [2]J. Ebner et al., J Proteomics, 2015, 117, 41–57. [3]F. C. Church et al., Journal of Dairy Science, 1983, 66 (6), 1219–1227. Volume77, IssueS3Supplement: Abstracts der Vorträge, Posterflashtalks und Poster von den 51. Deutschen Lebensmittelchemietagen 2023August 2023Pages S3-067-S3-067 ReferencesRelatedInformation

LebensmittelchemieVolume 77, Issue S3 p. S3-085-S3-085 Analytik Analysis of the peptide profile of pasteurized milk during storage E. Gardill, E. Gardill Erlangen/DSearch for more papers by this authorJ. Stützer, J. Stützer Erlangen/DSearch for more papers by this authorN. Zenk, N. Zenk Erlangen/DSearch for more papers by this authorDr. S. Dalabasmaz, Dr. S. Dalabasmaz Erlangen/D Lehrstuhl für Lebensmittelchemie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Straße 10, Erlangen/DSearch for more papers by this author E. Gardill, E. Gardill Erlangen/DSearch for more papers by this authorJ. Stützer, J. Stützer Erlangen/DSearch for more papers by this authorN. Zenk, N. Zenk Erlangen/DSearch for more papers by this authorDr. S. Dalabasmaz, Dr. S. Dalabasmaz Erlangen/D Lehrstuhl für Lebensmittelchemie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Straße 10, Erlangen/DSearch for more papers by this author First published: 01 August 2023 https://doi.org/10.1002/lemi.202359066AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat No abstract is available for this article. References [1]H. C. Deeth, M. J. Lewis, High Temperature Processing of Milk and Milk Products 2017, 15–39. [2]H. C. Deeth, M. J. Lewis, High Temperature Processing of Milk and Milk Products 2017, 177–260. [3]S. Dalabasmaz, M. Pischetsrieder, Comprehensive Foodomics 2021, 651–665. [4]S. Dalabasmaz et al., J. Proteom. 2019, 103444. Volume77, IssueS3Supplement: Abstracts der Vorträge, Posterflashtalks und Poster von den 51. Deutschen Lebensmittelchemietagen 2023August 2023Pages S3-085-S3-085 ReferencesRelatedInformation

Hop is widely used in beer brewing and as a medicinal product. The present study comprehensively analyzed the main molecular determinants of the antibacterial activity of hop extracts. Minimum inhibitory concentrations (MIC) against Bacillus subtilis between 31.25 and 250 mu g/mL were found in the ethanolic extracts of five hop varieties for beer brewing, but not in the tea hop sample. Activity-guided fractionation revealed the highest antibacterial activity for lupulone and adlupulone (MIC 0.98 mu g/mL). Metabolome profiling and subsequent multistep statistical analysis detected 33 metabolites out of 1826 features to be associated with the antibacterial activity including humulone, adhumulone, colupulone, lupulone, and adlupulone. Xanthohumol, the three humulone- and three lupulone congeners were quantified in the hop extracts by a validated ultrahighperformance liquid chromatography-mass spectrometry method. Considering concentrations and MICs, colupulone and lupulone were identified as major contributors to the antibacterial activity of hop extract with the highest antibacterial activity values (concentration/MIC) of 1.59 and 2.56.