Les Maîtres de l’Orge: The Proteome Content of Your Beer Mug

Fasoli, Elisa; Aldini, Giancarlo; Regazzoni, Luca; Kravchuk, Alexander V.; Citterio, Attilio; Righetti, Pier Giorgio

doi:10.1021/pr100551n

Cited by 72 publications

(85 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Among 30 proteins from Hordeum vulgare, α-amylase inhibitors, γ-hordein and a globulin from Triticum aestivum were identified by using isoelectric focusing in solution followed by 2DE (Konecna et al, 2012). In another study, the ProteoMiner-like fractionation step was incorporated with combinatorial peptide ligand libraries designed for beer proteins before gel electrophoresis (Fasoli et al, 2010). γ-Hordein 3 and a fragment of the α-amylase inhibitor were among the 20 proteins identified in beer.…”

Section: Mass Spectrometrymentioning

confidence: 99%

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Products¹

2014

EFS2

115

View full text Add to dashboard Cite

Following a request from the Food Safety Authority of Ireland, the EFSA Panel on Dietetic Products, Nutrition and Allergies (NDA Panel) was asked to deliver a scientific opinion on the evaluation of allergenic foods and food ingredients for labelling purposes. In view of the request, the NDA Panel decided to update its previous opinions relative to food ingredients or substances with known allergenic potential listed in Annex IIIa of 2003/89/EC, as amended. These include cereals containing gluten, milk and dairy products, eggs, nuts, peanuts, soy, fish, crustaceans, molluscs, celery, lupin, sesame, mustard and sulphites. The opinion relates to immunoglobulin (Ig)E-and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food. It includes information on the prevalence of food allergy in unselected populations, proteins identified as food allergens, cross-reactivities, the effects of food processing on the allergenicity of foods and ingredients, methods for the detection of allergens and allergenic foods, doses observed to trigger adverse reactions in sensitive individuals and risk assessment methodologies that have been used to derive individual and population thresholds for selected allergenic foods. The present opinion relates to immunoglobulin (Ig)E-and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food. For each food ingredient or substance listed in Annex IIIa, it includes information on the prevalence of food allergy in unselected populations, on proteins identified as food allergens, on cross-reactivities, on the effects of food processing on the allergenicity of foods and ingredients, on methods for the detection of allergens and allergenic foods, and on doses observed to trigger adverse reactions in sensitive individuals.Immune-mediated adverse reactions to foods manifest with clinical signs and symptoms of variable severity and duration, which may affect different organs and systems. Anaphylactic reactions to food are IgE mediated and may occur at any age. Non-IgE-mediated food allergy includes a wide range of diseases, including protein-induced enterocolitis and eosinophilic oesophagitis.A careful family and clinical history are the basis for diagnosis of food allergy. Food diaries, skin prick tests (SPTs), allergen-specific IgE measurements, food elimination diets and food challenges are part of the standard protocol for the diagnosis of food allergy. A positive SPT indicates sensitisation to the tested food, but it is not diagnostic of food allergy. Allergen-specific serum IgE antibodies similarly denote sensitisation to a particular food, but they are not diagnostic without a clinical history or food challenge. The use of atopy patch tests for the diagnosis of food allergy is controversial. Other available tests have no current role in the diagnosis of food allergy. Diag...

show abstract

Section: Mass Spectrometrymentioning

confidence: 99%

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Products¹

2014

EFS2

115

View full text Add to dashboard Cite

show abstract

“…The authors performed capture of proteins at three different pH values and were able to identify 322 proteins, of which 190 could only be found in the CPLL-treated samples (Fasoli et al, 2011a). CPLL were also applied for analyses of some plant-derived products (D'Amato et al, 2010(D'Amato et al, , 2011Fasoli et al, 2010aFasoli et al, , 2011bFasoli et al, , 2012. However, although ProteoMiner has been on the market for 5 years, this technology has still not entered plant research.…”

mentioning

confidence: 99%

Looking Deep Inside: Detection of Low-Abundance Proteins in Leaf Extracts of Arabidopsis and Phloem Exudates of Pumpkin

et al. 2012

View full text Add to dashboard Cite

The field of proteomics suffers from the immense complexity of even small proteomes and the enormous dynamic range of protein concentrations within a given sample. Most protein samples contain a few major proteins, which hamper in-depth proteomic analysis. In the human field, combinatorial hexapeptide ligand libraries (CPLL; such as ProteoMiner) have been used for reduction of the dynamic range of protein concentrations; however, this technique is not established in plant research. In this work, we present the application of CPLL to Arabidopsis (Arabidopsis thaliana) leaf proteins. One-and two-dimensional gel electrophoresis showed a decrease in high-abundance proteins and an enrichment of less abundant proteins in CPLL-treated samples. After optimization of the CPLL protocol, mass spectrometric analyses of leaf extracts led to the identification of 1,192 proteins in control samples and an additional 512 proteins after the application of CPLL. Upon leaf infection with virulent Pseudomonas syringae DC3000, CPLL beads were also used for investigating the bacterial infectome. In total, 312 bacterial proteins could be identified in infected Arabidopsis leaves. Furthermore, phloem exudates of pumpkin (Cucurbita maxima) were analyzed. CPLL prefractionation caused depletion of the major phloem proteins 1 and 2 and improved phloem proteomics, because 67 of 320 identified proteins were detectable only after CPLL treatment. In sum, our results demonstrate that CPLL beads are a time-and cost-effective tool for reducing major proteins, which often interfere with downstream analyses. The concomitant enrichment of less abundant proteins may facilitate a deeper insight into the plant proteome.

show abstract

“…2B, D, E). These proteins would potentially remain in the final beer, and have indeed been detected in beer (6)(7)(8)31). This clear distinction in temperature sensitivity between pools of the same protein suggested that covalent modifications may be driving diversity of protein structure and behaviour.…”

Section: Protein Modification Drives Stabilitymentioning

confidence: 97%

“…shown that the wort and beer proteome is highly complex, and contains hundreds of unique proteins from barley and yeast (6)(7)(8)(9)(10). Complex post-translational modifications including proteolysis, oxidation, and glycation are also present on proteins in wort and beer (8,11,12).…”

Section: Introductionmentioning

confidence: 99%

Post-translational modifications drive protein stability to control the dynamic beer brewing proteome

Kerr

Schulz

2018

Preprint

View full text Add to dashboard Cite

Mashing is a key step in beer brewing in which starch and proteins are solubilized from malted barley in a hot water extraction and digested to oligomaltose and free amino nitrogen. We used SWATH-MS to measure the abundance and site-specific modifications of proteins throughout a small-scale pale ale mash. Proteins extracted from the malt at low mash temperatures decreased precipitously in abundance at higher temperatures due to temperature-induced unfolding and aggregation.Correlation analysis of temperature-dependent abundance showed that sequence and structure were the main features that controlled protein abundance profiles. Partial proteolysis by barley proteases was common early in the mash. The resulting proteolytically clipped proteins were particularly temperature sensitive and were preferentially lost at high mash temperatures, while intact proteins remained soluble.

show abstract

Les Maîtres de l’Orge: The Proteome Content of Your Beer Mug

Cited by 72 publications

References 23 publications

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Looking Deep Inside: Detection of Low-Abundance Proteins in Leaf Extracts of Arabidopsis and Phloem Exudates of Pumpkin

Post-translational modifications drive protein stability to control the dynamic beer brewing proteome

Contact Info

Product

Resources

About