29 results on '"Nebbia S"'
Search Results
2. Effect of thermal processing on IgE cross-recognition of insect proteins in Italian patients allergic to house dust mite, shrimp and mealworm
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Cirrincione S, Lamberti C, Nebbia S, Brussino L, Giorgis V, Giuffrida MG, Rolla G, and Cavallarin L
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crossallergenicity ,food allergy ,fungi ,edible insects - Abstract
INTRODUCTION. Edible insects are considered a promising and sustainable alternative protein source for humans, able to meet the increasing world's nutritional needs. The possible diffusion of insect farming and commercialization in Europe, has prompted the scientific community to investigate the allergenicity risk associated to insect consumption (1,2). Considering that edible insects are generally consumed after thermal processing, it is crucial to assess how processing may modify the protein structure, thus altering the protein cross-reactivity. In this study, we present one of the first investigations on insect cross-allergenicity, in three groups of Italian patients with a convincing history of house dust mite and shrimp allergy and with primary respiratory and food sensitization to mealworm. METHODS. We investigated by immunoblotting, the effect of boiling (5 min at 100 °C) and frying (3 min at 180 °C in sunflower oil) on the IgE-binding capacities towards both soluble and insoluble proteins fractions from five edible insects (mealworm, buffalo worm, silkworm, cricket and grasshopper). The immune-reactive proteins were identified by LC-MS/MS. RESULTS. Our data suggest that, depending on the nature of the reactive protein, the cross-reactivity resulted to be affected in different ways according to the different types of processing. In general, thermal processing influences the protein solubility, resulting in a protein shift from water-soluble to water-insoluble fractions, a shift that is more marked after frying than after boiling. Among the immune-reactive proteins, tropomyosin shows to have an important role as a cross-allergen for house dust mite and shrimp allergic patients and to be heat-stable in both fried and boiled samples. Actually, tropomyosin is considered a pan-allergen in crustaceans, mollusks, mites and insects, due to the high similarity of its amino acid sequences among species (3,4). The larval cuticle protein seems to play a major role in the cross-reactivity of patients primarily sensitized to mealworm. CONCLUSION. On the basis of our results, the effects of processing appeared to be protein-, species- and treatment-specific. Therefore, for patients allergic to house dust mite, shrimp and mealworm the consumption of insects, even after thermal processing, requires some caution.
- Published
- 2020
3. Different roasting hazelnut procedures alter the structure of the protein bodies and affect the binding capacities of IgEs from allergic children
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Lamberti C, Nebbia S, Cirrincione S, Antoniazzi S, Manfredi M, Balestrini R, Monti G, Giuffrida MG, and Cavallarin L.
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food allergy ,hazelnut ,processing - Abstract
INTRODUCTION Thermal processing, commonly used during food production, may affect food allergenicity by inducing physical and/or chemical changes in proteins and lipids. However, due to the lack of detailed information on processing procedures, available evidences on this topic are presently contradictory. The aim of this study was to investigate how two different roasting techniques, hot air (HA) and infrared (IR), could modify the hazelnut seed structure, the protein profiles and solubility. Moreover, the ability of the IgEs from hazelnut allergic children to bind hazelnut proteins before and after roasting was evaluated. METHODS Experiments were designed on an Italian variety of C. avellana (Cv. Tonda Gentile delle Langhe) obtained from experimental fields. Two pilot-scale ovens infrared (IR) and hot air (HA) and two combinations of time and temperature for each oven were considered: 140 °C for 25 min (low temperature (LT)) and 170 °C for 17 min (high temperature (HT)) in HA; 140 °C for 12 min (LT) and 170 °C for 10 min (HT) in IR. RESULTS A decrease in hazelnut protein solubility was detectable following LT-IR roasting and it became more evident after HT processing, for both roasting types. The immuno-recognition decreased progressively from raw to high temperature processes. The IR-HT processing caused a quite complete disappearance of immune-recognition of hazelnut proteins. Interestingly, different allergens showed different responses to heat processing. The immune-reactivity of Cor a 9, Cor a 11 and Cor a 14 resulted to be stable until 140 °C, while Cor a 8 immuno-recognition was already reduced at 140 °C and completely lost at 170 °C. Differently, oil body (OB) associated protein immuno-recognition was increased after HA roasting at 140 °C whereas was reduced in the remaining treatments and disappeared in the IR-HT. At structural level, microscopical observations showed a cytoplasmic network disruption with an alteration of the structure of the protein bodies and of the cell wall organization. CONCLUSION IR oven is the least conservative processing, especially at high temperatures, both considering protein solubility and immuno-recognition. Our results could be useful for the development of clinical protocols for the process of oral desensitization of hazelnut allergic patients.
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- 2020
4. Identification of a caleosin associated with hazelnut (Corylus avellana L.) oil bodies
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Lamberti, C., primary, Nebbia, S., additional, Balestrini, R., additional, Marengo, E., additional, Manfredi, M., additional, Pavese, V., additional, Cirrincione, S., additional, Giuffrida, M. G., additional, Cavallarin, L., additional, Acquadro, A., additional, and Abbà, S., additional
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- 2020
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- View/download PDF
5. Impact of HTST pasteurization of human milk on the kinetic of digestion of macronutrients after in vitro dynamic digestion
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Nebbia, S., Gribaldi, M., Cavallarin, L., Coscia, A., Ménard, Olivia, Dupont, Didier, Deglaire, Amélie, Institute of Sciences of Food Production (ISPA), Consiglio Nazionale delle Ricerche (CNR), Unité de Néonatologie, Université de Turin, Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), infogest, and Institut National de Recherche Agronomique (INRA). UMR UMR INRA / AgroCampus Rennes : Science et Technologie du Lait et de l'?uf (1253).
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cinétique de digestion ,pasteurizing ,mesure d'impact ,HTST ,enfant prématuré ,innovation alimentaire ,human milk ,pasteurisation ,digestion ,allégations nutritionnelles et de santé ,premature infant ,high temperature ,milk protein ,digestion in vitro ,protéine du lait ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,peptide du lait ,haute température ,[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition ,évaluation de l'impact ,lait humain - Abstract
Donor human milk (DHM) represents the best alternative when mother’s own milk is not available,a common occurrence in Neonatal Intensive Care Units. Heat treatment of DHM is mandatory forsafety reasons. Holder pasteurization (HoP, 62.5°C-30’) is recommended by all human milk bankguidelines. Recent studies have demonstrated that HoP affects the digestion profile and behavior ofseveral human milk components. High Temperature-Short Time pasteurization (HTST, 71°C-15’’)is currently under evaluation as a promising alternative technology to limit the denaturation of somebiological compounds of raw human milk.ObjectiveThe aim of the present work was to assess whether the different types of pasteurization (HoP,HTST) impacted the digestive kinetics of human milk during in vitro dynamic digestion.MethodologyPooled raw HM (RHM) was collected and processed by using the two pasteurization techniques.The pasteurized samples and RHM were digested in vitro using preterm gastrointestinal conditions.Samples were collected at different digestion times. Undigested and digested milks samples werecharacterized for their particle size distribution (PSD), triglyceride content, protein and amino acid(AA) profiles.Main findingsDuring gastric digestion, both pasteurization methods modified PSD, as compared to RHM. Caseinswere rapidly hydrolyzed in the gastric phase unlike that for the whey proteins. Lactoferrin was hydrolyzedfaster in the pasteurized samples in comparison to RHM, in which lactoferrin was resistantto gastro-intestinal digestion. Heat-treatments, consequently, affected the intestinal release of someAA, and a higher bioaccessibility of AA was found for HTST, as compared to HoP. Concerning lipolysis,at any time of the intestinal digestion phase, the lipolysis of HoP samples was significantlylower (p < 0.05) than in both RHM and HTST samples.ConclusionThis work provides the first evidences about the differential impact of HoP and HTST pasteurizationtechniques on bioaccessibility of DHM nutrients and biological compounds, for preterm newborns.
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- 2019
6. Do different techniques of human milk pasteurization impact the kinetics of peptide release during in vitro dynamic digestion?
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Gribaldi, M., Nebbia, S., Cavallarin, L., Sottemano, S., Briard-Bion, Valérie, Jardin, Julien, Ménard, Olivia, Dupont, Didier, Deglaire, Amélie, Institute of Sciences of Food Production (ISPA), Consiglio Nazionale delle Ricerche (CNR), Unité de Néonatologie, Université de Turin, Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, infogest, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), and Institut National de Recherche Agronomique (INRA). UMR UMR INRA / AgroCampus Rennes : Science et Technologie du Lait et de l'?uf (1253).
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cinétique de digestion ,mesure d'impact ,pasteurizing ,innovation alimentaire ,enfant prématuré ,human milk ,pasteurisation ,digestion ,allégations nutritionnelles et de santé ,premature infant ,milk protein ,digestion in vitro ,protéine du lait ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,peptide du lait ,[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition ,lait humain ,évaluation de l'impact - Abstract
IntroductionIn order to minimize the denaturation of bioactive compounds, which is known to affect donor humanmilk (HM) after the mandatory heat treatment (Holder pasteurization at 62.5°C, 30min – HoP), anumber of alternative processing techniques are currently being investigated. Recently, High Temperature-Short Time pasteurization (HTST, 72°C-15s) was found to limit the denaturation of somebioactive components of human milk.ObjectiveThe aim of the study was to investigate whether different types of pasteurization (HoP and HTST)may differently affect peptide release from human milk during preterm infant gastrointestinal digestion,by using a dynamic in vitro systemMethodologyPooled raw HM (RHM) from 5 donors was collected and processed in triplicate according to HoP andHTST. The pasteurized milks and RHM were digested in triplicate using a dynamic in vitro digestionsystem, mimicking the preterm physiology conditions. Samples were collected at different digestiontimes. Peptides from undigested and digested samples were analysed using a Q-Exactive massspectrometer and peptide abundance was subjected to multivariate statistics to unravel specificprofile trends.Main findingsPre-proteolysis occurred mostly on β-casein, from which originated more than 82% of the peptidesfound in undigested milk. During digestion, a differential behaviour between gastric and intestinalpeptide release was found by multivariate statistics. In particular, whereas in the gastric phase thepeptide pattern was more similar for HTST and RHM with respect to HoP, the opposite was found atthe beginning of the intestinal phase, while at the end of digestion no difference was found. Thesedifferences were mostly due to peptides released from β-casein, especially in the gastric phase.Some bioactive peptides from bile salt-stimulated lipase, caseins and lactoferrin presented significantlydifferent abundances between the different samples during intestinal digestion.ConclusionThe results indicate possible consequences of the different pasteurizations on the biological activityof donor’s human milk.
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- 2019
7. Effect of different types of roasting on hazelnut immunoreactivity
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Lamberti C.(1), Nebbia S.(1), Cirrincione S. (1), Antoniazzi S.(1), Manfredi M.(2), Marengo E.(2), Giuffrida M.G.(1), and Cavallarin L. (1)
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food allergy ,hazelnut ,processing - Abstract
Introduction: It is known that thermal processing, commonly used during food production, may affect food allergenicity by inducing physical and/or chemical changes in macronutrients. However, due to the lack of detailed information on processing procedures, available evidences on this topic are presently contradictory. This study aims to evaluate the effects of different types of roasting on hazelnut protein solubility and immune reactivity. Methods: We investigated the IgE-binding capacities of both soluble and insoluble hazelnut protein fractions from C. avellana (Cv. Tonda Gentile delle Langhe), before and after roasting using two different roasting techniques: hot air (HA) as a ''traditional method," and infrared (IR), as an ''innovative method". Two combinations of time and temperature for each oven were considered: 140°C for 25min (LT) and 170°C for 17 min (HT) in HA; 140°C for 12 min (LT) and 170°C for 10 min (HT) in IR. Total protein and oil body associated protein extracts were used for immunoblotting experiments with allergic patient sera. Results: A decrease in hazelnut protein solubility was detectable following LT-IR roasting and it became more evident after HT processing, for both roasting types. Concerning allergenicity, the raw hazelnut proteins extract was the most immune reactive, followed by LT-HA and LT-IR processed hazelnut that showed a very similar immune reactive pattern. The HA-HT treatment resulted in a low, although detectable, immune reactivity, while the IR-HT processing caused a quite complete disappearance of immune reactivity of hazelnut proteins. The different hazelnut allergens (Cor a 8, 9, 11, 12, 13, 14, 15) were differently affected by thermal treatments, in accordance with their thermal stability, as already reported by literature. Discussion: HA oven is the most conservative processing, especially at low temperatures, both considering protein solubility and immune-reactivity. Both the HT treatments demonstrated to reduce immune-recognition of hazelnut proteins by allergic patient sera.
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- 2019
8. Effect of thermal processing on the immune cross-reactivity of five edible insects
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Cirrincione S. (1), Nebbia S. (1), Lamberti C. (1), Bufo A. (1), Giorgis V. (2), Manfredi M. (3), Marengo E. (3), Giuffrida M.G. (1), Rolla G. (2), and Cavallarin L. (1)
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food allergy ,edible insect ,cross-reactivity ,fungi ,LC-MS/MS - Abstract
Introduction. Edible insects are currently being evaluated as an alternative and sustainable protein source for humans in order to meet the nutritional needs of the growing world population. Specific risk assessment for edible insects is necessary in Europe, where the consumption of insects is an emerging practice. The allergenic potential associated to entomophagy has to be investigated since the introduction of this new food source can cause IgE-mediated cross reactions in patients allergic to crustaceans and mites, that belong to the same phylum of insect. Methods. Five edible insects were investigated: buffalo worm (Alphitobius diaperinus), mealworm (Tenebrio molitor), silkworm (Bombyx mori); cricket (Gryllodes sigillatus) and grasshopper (Locusta migratoria). The soluble and insoluble proteins were extracted from raw and processed (boiled and fried) insects and the protein profiles were analyzed by SDS-PAGE. The IgE cross-reactivity of shrimp (n=8) and house dust mite (n=28) Italian allergic patients were investigated by immunoblotting followed by LC-MS/MS analysis for immune-reactive proteins identification. Results. Buffulo worm, mealworm and cricket showed similar protein profiles for raw and boiled extract, while grasshopper and silkworm differed for both processing methods. For all insects, proteins aggregation increased with increasing processing temperatures, causing an enrichment of the insoluble protein fraction. Preliminary results on the immune-recognition of insect proteins by the sera IgEs of patient allergic to shrimp and mites indicate that the major allergens of shrimp and house dust mite, such as tropomyosin and arginine kinase, are cross-reactive in insects. Furthermore, both processing methods show to affect protein reactivity in an insect-dependent manner. Discussion. The evidence of cross-reactivity of IgEs from patients allergic to shrimp and house dust mite towards differently processed edible insect protein extracts confirms the issue of possible risk associated to insects consuming.
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- 2019
9. Fortification du lait de femme à base de protéines de lait d'ânesse ou de vache: impact sur la digestion du prématuré en condition in vitro
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Nebbia S., Giribaldi M., Bertino E., Coscia A., Ménard O., Cavallarin L., Deglaire A., and Dupont D.
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fortifiers ,human milk ,donkey milk ,preterm infants ,digestion ,proteins - Published
- 2019
10. A case of two allergic patients sensitized to Tenebrio molitor by occupational exposure
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Lamberti, C., Nebbia, S., Giorgis, V, Fornero, M., Giuffrida, M. G., Rolla, G., and Cavallarin, L.
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insect proteins ,allergy - Published
- 2018
11. Characterization of allergy to hazelnut oleosins in pediatric patients in Italy
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Nebbia, S., Lamberti, C., Bua, A., Manfredi, M., Marengo, E., Monti, G., Cavallarin, L., and Giuffrida, M. G.
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oleosins ,allergy - Published
- 2018
12. Identification of 30 KDa Bombyx mori allergen by immunoblotting and MALDI-TOF/TOF mass spectrometry
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Nebbia S.(1), Purrotti M.(1), Lamberti C.(1), Gai F.(1), Salierno I.(1), Saviane A.(2), Cappellozza S.(2), Rolla G.(3), Giorgis V.(3), Giuffrida M.G.(1), and Cavallarin L.(1)
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bombyx mori ,food allergy ,fungi ,mass spectrometry - Abstract
Edible insects can be a source of sustainable protein with low environmental impact. Among them, the silkworm (Bombyx mori) pupae (SWP) has been included in the EFSA (European Food Safety Authority) list of insect species with a interesting food application. Insects are a traditionally food in East and Southeast Asia and every year in China 1000 people have allergic reaction after SWP ingestion. In the Europe the introduction of insect into the diet will take place after study of specific risk assessment, including the evaluation of the allergenic potential. The aim of this work was to evaluate the allergenicity of SWP by immunoblotting performed with the sera of two patient sensitized during manipulation of insect flour and to identify the immuno-reactive proteins with mass spectrometry approach. Total proteins extract were separated by SDS-PAGE and transferred into nitrocellulose membrane. The membranes were incubated o.n. with the two sensitized patient sera. The immune-complex was detected with anti-human IgE AP Conjugate antibody. The reactive band was cut from the gel, destained and digested by trypsin (o.n., at 37°C) and the resulting peptides were analyzed by MALDI-TOF/TOF. On the three more relevant piques were performed the Post Source Decay(PSD) analysis. The mass spectra were analyzed by Flex Analysis software and the m/z list were used by Protein Prospector search software (MS-Fit and MS-Tag)to query UniProt data base. The Immunoblotting results show only one reactive band for both the sensitized patients. The identification show different protein belonging of 30Kda Lipoprotein family, one of the most abundant protein in SWP hemolymph. This is a defense protein and it's already known to be a food allergen. This preliminary study about SWP allergenicity could improve the state-of-the-art about edible insect safety from the allergenic point of view. It's one of the first evaluation of SWP allergenic potential using the sera of two Italian patient sensitized during manipulation of insect flour; a rare case of allergy to insect proteins in Europe.
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- 2017
13. A Case of Work-Related Donkey Milk Allergy
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Giorgis, V, primary, Rolla, G, additional, Raie, A, additional, Geuna, M, additional, Boita, M, additional, Lamberti, C, additional, Nebbia, S, additional, Giribaldi, M, additional, Giuffrida, MG, additional, Brussino, L, additional, Corradi, F, additional, Bacco, B, additional, Gallo Cassarino, S, additional, Nicola, S, additional, and Cavallarin, L, additional
- Published
- 2018
- Full Text
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14. Bioactive peptides produced by LAB of food interest
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Cirrincione S., Nebbia S., Giuffrida M.G., Cavallarin L., Laroute V., and Pessione E.
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not available - Abstract
Not available
- Published
- 2016
15. Pepti-Donk: enhancement of piedmontese donkey milk as nutraucetical food
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Cirrincione S, Terlizzi ME, Nebbia S, Cavallarin L, Giuffrida MG, and Pessione E
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not available - Abstract
Not available
- Published
- 2016
16. Le carte dell’abbazia di S.Bartolomeo di Azzano (952, 1151-1335)
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Fissore, Gian Giacomo, Cotto, A. M., and Nebbia, S.
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- 1997
17. Peptidomic profile of human milk as influenced by fortification with different protein sources: An in vitro dynamic digestion simulation.
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Giribaldi M, Nebbia S, Briard-Bion V, Jardin J, Ménard O, Dupont D, Coscia A, Cresi F, Lamberti C, Cavallarin L, and Deglaire A
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- Humans, Animals, Cattle, Food, Fortified analysis, Tandem Mass Spectrometry, Models, Biological, Whey Proteins chemistry, Whey Proteins metabolism, Milk, Human chemistry, Milk, Human metabolism, Equidae, Milk Proteins chemistry, Milk Proteins metabolism, Milk Proteins analysis, Peptides chemistry, Peptides metabolism, Digestion
- Abstract
Fortification of human milk (HM) is often necessary to meet the nutritional requirements of preterm infants. The present experiment aimed to establish whether the supplementation of HM with either an experimental donkey milk-derived fortifier containing whole donkey milk proteins, or with a commercial bovine milk-derived fortifier containing hydrolyzed bovine whey proteins, affects peptide release differently during digestion. The experiment was conducted using an in vitro dynamic system designed to simulate the preterm infant's digestion followed by digesta analysis by means of LC-MS-MS. The different fortifiers did not appear to influence the cumulative intensity of HM peptides. Fortification had a differential impact on the release of either donkey or bovine bioactive peptides. Donkey milk peptides showed antioxidant/ACE inhibitory activities, while bovine peptides showed opioid, dipeptil- and propyl endo- peptidase inhibitory and antimicrobial activity. A slight delay in peptide release from human lactoferrin and α-lactalbumin was observed when HM was supplemented with donkey milk-derived fortifier., Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Laura Cavallarin has patent #Food Composition - EP 3057450 B1 issued to n.a. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)
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- 2025
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18. In vitro gastrointestinal digestion of cow's and sheep's dairy products: Impact of species and structure.
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Saviard T, Menard O, Nebbia S, Ossemond J, Henry G, Chacon R, Le Feunteun S, Dupont D, and Le Roux L
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- Animals, Cattle, Sheep, Lactoglobulins metabolism, Gastrointestinal Tract metabolism, Dairy Products analysis, Lactalbumin metabolism, Caseins metabolism, Caseins analysis, Species Specificity, Milk Proteins analysis, Milk Proteins metabolism, Digestion physiology, Yogurt analysis, Milk chemistry, Lipolysis, Proteolysis, Particle Size
- Abstract
Sheep's milk (SM) is known to differ from cow's milk (CM) in nutritional composition and physicochemical properties, which may lead to different digestion behaviours. This work aimed to investigate the impact of the species (cow vs sheep) and the structure (milk vs yogurt) on the digestion of dairy products. Using an in vitro static gastrointestinal digestion model, CM, SM, cow's milk yogurt (CY) and sheep's milk yogurt (SY) were compared on particle size evolution, microscopic observations, degree of lipolysis, degree of proteolysis, specific protein degradation and calcium bioaccessibility. Species and structure affected particle size evolution during the gastric phase resulting in smaller particles for yogurts compared to milks as well as for CM products compared to SM products. Species impacted lipid composition and lipolysis, with SM products presenting higher short/medium-chain fatty acids content and higher intestinal degree of lipolysis. Proteolysis was influenced by structure, with milks showing higher intestinal degree of proteolysis compared to yogurts. Caseins were digested faster in CM, ⍺-lactalbumin was digested faster in SM despite its higher concentration, and during gastric digestion β-lactoglobulin was more degraded in CM products compared to SM products and more in yogurts compared to milks. Lastly, SM products released more bioaccessible calcium than CM products. In conclusion, species (cow vs sheep) impacted more the digestion compared to the structure (milk vs yogurt). In fact, SM was different from CM mainly due to a denser protein network that might slow down the accessibility of the enzyme to its substrate which induce a delay of gastric disaggregation and thus lead to slower the digestion of the nutrients., Competing Interests: Declaration of competing interest Tanguy Saviard, Linda Le Roux, and Raphaël Chacon are employees of Sill Entreprises. Other authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)
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- 2024
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19. Impact of process and composition of formulas for elderly on in vitro digestion using the dynamic DIDGI® model.
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Nebbia S, Ménard O, Cochet MF, Henry G, Daniel N, Moran L, Lennon K, Dollard G, Moloney C, Collins M, Morgan F, and Dupont D
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- Humans, Aged, Animals, Milk metabolism, Lipolysis, Plant Oils metabolism, Digestion, Gastrointestinal Diseases
- Abstract
Due to the lower efficiency of the elderly digestion system, new formulations are needed in order to increase the bioaccessibility of macronutrients. The aim of the work was to evaluate the effect of the process of protein sources production using either liquid (F2) vs spray dried milk proteins (F1/F3) and the source of lipids (vegetable oil (F1) vs mix of vegetable oil + bovine milk cream (F2/F3)) ingredients on the macronutrient digestion of three experimental elderly formulas. The dynamic in vitro digestion model DIDGI®
, was adapted to simulate the digestive conditions of the elderly. An exhaustive review of the literature was carried out in order to simulate as closely as possible the elderly digestive parameters and constituted the starting point towards a consensus in vitro digestion model that will be proposed soon by the INFOGEST scientific network. The three experimental formulas (F1/F2/F3) differing by the composition and process applied were submitted to the DIDGI® dynamic in vitro digestion over four hours using parameters adapted to the elderly. The three formulas were compared in terms of proteolysis and lipolysis. A slight impact of the process (liquid vs spray-dried) on the degree of proteolysis at the end of digestion was observed with 50.8% for F2 compared to 56.8% for F1 and 52.9% for F3 with<5% of difference between the 3 formulas. Concerning the degree of lipolysis, the addition of bovine cream led to a lesser extent of lipolysis with 63.7 and 60.2% for F2 and F3 respectively versus 66.3% for F1 (containing only vegetable oil). Our results highlighted the beneficial input of the milk fat with a higher level of phospholipids and a lower ω6/ω3 PUFA ratio and can be a good alternative to the use of the vegetable fat in drinks for elderly people., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier Ltd. All rights reserved.)- Published
- 2023
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20. Supplementing human milk with a donkey or bovine milk derived fortifier: Consequences on proteolysis, lipolysis and particle structure under in vitro dynamic digestion.
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Nebbia S, Deglaire A, Ménard O, Henry G, Barberis E, Manfredi M, Bertino E, Coscia A, Dupont D, Giribaldi M, and Cavallarin L
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- Animals, Digestion, Equidae, Food, Fortified, Humans, Infant, Infant, Newborn, Lipolysis, Proteolysis, Infant, Premature, Milk, Human chemistry
- Abstract
Fortification of human milk (HM) is often necessary to meet the nutritional requirements of preterm infants. This study sought to establish whether HM supplemented with an experimental donkey milk-derived fortifier (DMF) or a commercial bovine milk-derived fortifier (BMF) affected digestion, using an in vitro dynamic system at the preterm stage. Particle size in gastric phase was higher in DMF than in BMF, due to protein aggregates surrounding lipid globules. Before digestion, BMF, with its extensively hydrolysed proteins, had a higher degree of proteolysis (30%) than DMF (11%), which contained intact proteins. After digestion, this difference was reduced concomitantly to a similar net degree of proteolysis (33%). DMF, with a higher proportion of ω3, resulted in a lower ω6/ω3 free PUFA ratio than BMF throughout digestion, although the final degree of lipolysis was similar (54%). In summary, DMF could represent a better source of proteins and lipids for the preterm infant., (Copyright © 2022 Elsevier Ltd. All rights reserved.)
- Published
- 2022
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21. Simulated dynamic digestion reveals different peptide releases from human milk processed by means of holder or high temperature-short time pasteurization.
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Giribaldi M, Nebbia S, Briard-Bion V, Jardin J, Peila C, Coscia A, Dupont D, Cavallarin L, and Deglaire A
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- Animals, Digestion, Humans, Infant, Infant, Newborn, Infant, Premature, Milk, Peptides, Temperature, Milk, Human, Pasteurization
- Abstract
High Temperature-Short Time (HTST) pasteurization was proposed as an alternative to Holder pasteurization (HOP) to increase the retention of specific human milk (HM) bioactive proteins. The present study explored whether HTST and HOP differently affect peptide release during simulated preterm infant gastrointestinal digestion. Raw (RHM), HOP- and HTST- pasteurized HM were digested using an in vitro dynamic system, and the identified peptides were analyzed by mass spectrometry and multivariate statistics. Before digestion, 158 peptides were identified in either RHM, HTST- or HOP- HM, mostly (84.4%) originating from β-casein (CASB). During gastric digestion, HOP-HM presented a greater number and more abundant specific CASB peptides. A delayed release of peptides was observed in RHM during the intestinal phase, with respect to both pasteurized HM. Although limited to gastric digestion, the HM peptidomic profile differed according to the pasteurization type, and the pattern of the HTST peptides showed a greater similarity with RHM., (Copyright © 2021 Elsevier Ltd. All rights reserved.)
- Published
- 2022
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22. Oleosin Cor a 15 is a novel allergen for Italian hazelnut allergic children.
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Nebbia S, Lamberti C, Cirrincione S, Acquadro A, Abbà S, Ciuffo M, Torello Marinoni D, Manfredi M, Marengo E, Calzedda R, Monti G, Cavallarin L, and Giuffrida MG
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- Allergens, Child, Humans, Immunoglobulin E, Italy, Plant Proteins, Proteomics, Corylus, Nut Hypersensitivity diagnosis
- Abstract
Background: Hazelnut allergy, which is characterized by symptoms that range from mild to severe, is one of the most common allergies in children throughout Europe, and an accurate diagnosis of this allergy is therefore essential. However, lipophilic allergens, such as oleosins, are generally underrepresented in diagnostic tests. We therefore sought to characterize the IgE reactivity of raw and roasted hazelnut oleosins, using the sera of hazelnut-allergic pediatric patients., Methods: Raw and roasted hazelnut oil body-associated proteins were analyzed by means of 1D and 2D electrophoresis and MS. Oleosin IgE reactivity was assessed by immunoblotting with the sera of 27 children who have confirmed hazelnut allergies and from 10 tolerant subjects. A molecular characterization of the oleosins was performed by interrogating the C. avellana cv. Jefferson and cv. TGL genomes, and through expression and purification of the recombinant new allergen., Results: A proteomic and genomic investigation allowed two new oleosins to be identified, in addition to Cor a 12 and Cor a 13, in hazelnut oil bodies. One of the new oleosins was registered as a new allergen, according to the WHO/IUIS Allergen Nomenclature Subcommittee criteria, and termed Cor a 15. Cor a 15 was the most frequently immunorecognized oleosin in our cohort. Oleosins resulted to be the only immunorecognized allergens in a subgroup of allergic patients who showed low ImmunoCAP assay IgE values and positive OFC and PbP. Hazelnut roasting resulted in an increase in oleosin immunoreactivity., Conclusion: A novel hazelnut oleosin, named Cor a 15, has been discovered. Cor a 15 could play a role in eliciting an allergic reaction in a subgroup of pediatric patients that exclusively immunorecognize oleosins. The high prevalence of hazelnut oleosin sensitization here reported further confirms the need to include oleosins in routine diagnostic procedures., (© 2021 The Authors. Pediatric Allergy and Immunology published by European Academy of Allergy and Clinical Immunology and John Wiley & Sons Ltd.)
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- 2021
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23. Thermal processing of insect allergens and IgE cross-recognition in Italian patients allergic to shrimp, house dust mite and mealworm.
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Lamberti C, Nebbia S, Cirrincione S, Brussino L, Giorgis V, Romito A, Marchese C, Manfredi M, Marengo E, Giuffrida MG, Rolla G, and Cavallarin L
- Subjects
- Allergens, Animals, Chromatography, Liquid, Humans, Immunoglobulin E, Insecta, Italy, Pyroglyphidae, Tandem Mass Spectrometry, Hypersensitivity, Tenebrio
- Abstract
Edible insects are considered as a promising and sustainable alternative protein source for humans, although risk assessments, with particular reference to the allergic potential of insect proteins, are required. Considering that insects are likely to be consumed after processing, it is crucial to assess how processing can influence allergenicity. In our study, we investigated how boiling and frying affect the IgE cross-recognition of proteins from five edible insects (mealworm, buffalo worm, silkworm, cricket and grasshopper). We considered three groups of Italian patients allergic to shrimps and to house dust mites, who had never consumed insects before and two subjects with occupational allergy and food sensitization to mealworm. Our data suggest that thermal processing may change the solubility of proteins, thereby resulting in a protein shift from water-soluble fractions to water-insoluble fractions. Immunoblot and LC-MS/MS analyses have shown that tropomyosin may play an important role as a cross-allergen for house dust mite and shrimp allergic patients, while larval cuticle protein seems to play a major role in the cross-reactivity of patients primarily sensitized to mealworm. On the basis of our results, the effects of processing appear to be protein-, species- and treatment-specific. Therefore, house dust mite, shrimp and mealworm allergic patients should consume insects with caution, even after thermal processing., (Copyright © 2021 Elsevier Ltd. All rights reserved.)
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- 2021
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24. Effect of hot air and infrared roasting on hazelnut allergenicity.
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Lamberti C, Nebbia S, Antoniazzi S, Cirrincione S, Marengo E, Manfredi M, Smorgon D, Monti G, Faccio A, Giuffrida MG, Balestrini R, and Cavallarin L
- Subjects
- Allergens chemistry, Child, Chromatography, High Pressure Liquid, Food Hypersensitivity blood, Food Hypersensitivity pathology, Hot Temperature, Humans, Immunoglobulin E blood, Immunoglobulin E immunology, Plant Proteins chemistry, Protein Stability, Tandem Mass Spectrometry, Allergens immunology, Cooking methods, Corylus metabolism, Infrared Rays, Plant Proteins immunology
- Abstract
Roasting is known to affect the protein profile and allergenicity of hazelnuts (Corylus avellana cv TGL). The aim of the study was to investigate whether roasting techniques based on different heat transfer methods (hot air and infrared), differently affect the protein solubility and the IgE-binding capacities of both the soluble and insoluble hazelnut protein fractions. The immune-reactivity of the Cor a 9, Cor a 11 and Cor a 14 allergens resulted to be stable after roasting at 140 °C, for both types of treatment, while roasting at 170 °C caused a reduction in IgE-binding, which was particularly noticeable after infrared processing, that led to an almost complete disappearance of allergenicity. Microscopical analyses showed that roasting caused cytoplasmic network disruption, with a loss of lipid compartmentalization, as well as an alteration of the structure of the protein bodies and of the cell wall organization., (Copyright © 2020. Published by Elsevier Ltd.)
- Published
- 2021
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25. Antimicrobial Potential of Food Lactic Acid Bacteria: Bioactive Peptide Decrypting from Caseins and Bacteriocin Production.
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Nebbia S, Lamberti C, Lo Bianco G, Cirrincione S, Laroute V, Cocaign-Bousquet M, Cavallarin L, Giuffrida MG, and Pessione E
- Abstract
Lactic acid bacteria (LAB) potential in the food industry and in the biotechnological sector is a well-established interest. LAB potential in counteracting especially food-borne infections has received growing attention, but despite being a road full of promises is yet poorly explored. Furthermore, the ability of LAB to produce antimicrobial compounds, both by ribosomal synthesis and by decrypting them from proteins, is of high value when considering the growing impact of multidrug resistant strains. The antimicrobial potential of 14 food-derived lactic acid bacteria strains has been investigated in this study. Among them, four strains were able to counteract Listeria monocytogenes growth: Lactococcus lactis SN12 and L. lactis SN17 by high lactic acid production, whereas L. lactis 41FLL3 and Lactobacillus sakei I151 by Nisin Z and Sakacin P production, respectively. Strains Lactococcus lactis MG1363 , Lactobacillus rhamnosus 17D10 and Lactobacillus helveticus 4D5 were tested and selected for their potential attitude to hydrolyze caseins. All the strains were able to release bioactive peptides with already known antimicrobial, antihypertensive and opioid activities. These features render these strains or their bioactive molecules suitable for use in food as biocontrol agents, or as nutraceutical supplements to treat mild disorders such as moderate hypertension and children insomnia. These results highlight once again that LAB potential in ensuring food safety, food nutraceutical value and ultimately in favoring human health is still underexplored and underexploited.
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- 2020
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26. Differential impact of Holder and High Temperature Short Time pasteurization on the dynamic in vitro digestion of human milk in a preterm newborn model.
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Nebbia S, Giribaldi M, Cavallarin L, Bertino E, Coscia A, Briard-Bion V, Ossemond J, Henry G, Ménard O, Dupont D, and Deglaire A
- Subjects
- Chromatography, High Pressure Liquid, Hot Temperature, Humans, Infant, Newborn, Infant, Premature, Lactoferrin chemistry, Mass Spectrometry, Proteolysis, Time Factors, Milk, Human chemistry, Pasteurization methods
- Abstract
The high-temperature short-time (HTST, 72 °C, 15 s) pasteurization of human milk (HM) has been proposed as an alternative to the Holder method (HoP, 62.5 °C, 30 min), to increase the preservation of bioactive compounds. We have investigated the impact of HTST and HoP pasteurization on the gastrointestinal kinetics of human milk, using a dynamic in vitro system in a preterm newborn model. An increased protein aggregation on the surface of fat globules following pasteurization, albeit to a lesser extent in HTST than in HoP, was observed. Despite relevant differences in the undigested milk samples, both pasteurization methods led to similar proteolytic patterns, while raw HM presented a higher native lactoferrin content throughout digestion. The slightly decreased amino acid release following HoP, with respect to HTST and raw HM, indicated that peptidomic analysis, which is currently underway, might provide interesting insights on the differential digestive kinetics of differently pasteurized HM., Competing Interests: Declaration of Competing Interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: MG, LC, EB and AC have competing interests, since they are the inventors of a patent pertaining to the HTST human milk pasteurizer used in the study (Patent no. EP2974603 A1). No conflict of interest exists for the remaining authors., (Copyright © 2020 Elsevier Ltd. All rights reserved.)
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- 2020
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27. The cockroach allergen-like protein is involved in primary respiratory and food allergy to yellow mealworm (Tenebrio molitor).
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Nebbia S, Lamberti C, Giorgis V, Giuffrida MG, Manfredi M, Marengo E, Pessione E, Schiavone A, Boita M, Brussino L, Cavallarin L, and Rolla G
- Subjects
- Adult, Animals, Humans, Male, Allergens immunology, Cockroaches immunology, Food Hypersensitivity diagnosis, Food Hypersensitivity immunology, Insect Proteins immunology, Tenebrio immunology
- Published
- 2019
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28. Enflurane decreases the threshold for vasoconstriction more than isoflurane or halothane.
- Author
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Nebbia SP, Bissonnette B, and Sessler DI
- Subjects
- Body Temperature Regulation drug effects, Child, Preschool, Female, Humans, Hypothermia chemically induced, Intraoperative Complications, Male, Anesthetics, Inhalation adverse effects, Enflurane adverse effects, Halothane adverse effects, Isoflurane adverse effects, Vasoconstriction drug effects
- Abstract
Intraoperative hypothermia results largely from anesthetic-induced inhibition of tonic thermoregulatory vasoconstriction. Sufficient hypothermia, however, triggers peripheral vasoconstriction, which usually prevents further decrease in core temperature. The thermoregulatory effects of all volatile anesthetics have been tested in adults and/or children, but different anesthetics have not been directly compared. We therefore evaluated thermoregulatory responses during enflurane, isoflurane, and halothane administration. Anesthesia was maintained with 1 minimum alveolar anesthetic concentration (MAC) of halothane, isoflurane, or enflurane in 27 patients undergoing intraabdominal surgery. Patients were maintained normovolemic and normocapnic but were allowed to cool passively. A forearm minus fingertip, skin-temperature gradient of 4 degrees C identified significant vasoconstriction; the core temperature triggering vasoconstriction identified the threshold. Morphometric characteristics, initial core temperatures, ambient operating room temperatures, blood pressures, and anesthetic potencies were similar in each group. All eight patients given halothane vasoconstricted at a core temperature of 35.5 +/- 0.6 degrees C. Eight of the patients given isoflurane vasoconstricted at a core temperature of 35.2 +/- 0.5 degrees C. However, two others did not at minimum core temperatures of 34.0 and 33.8 degrees C. Only one patient given enflurane vasoconstricted at a core temperature of 34.6 degrees C. The other six patients never vasoconstricted, at minimum core temperatures of 33.6 +/- 0.4 degrees C. Our data indicate that enflurane profoundly inhibits thermoregulatory responses in children. The mechanism for this extraordinary inhibition remains unknown but does not result from any obvious anesthetic pharmacology or thermoregulatory physiology. We conclude that unwarmed pediatric patients will become colder when anesthetized with enflurane than with halothane or isoflurane.
- Published
- 1996
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29. Intravenous dead space and patient safety in patient-controlled analgesia.
- Author
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Doyle DJ and Nebbia SP
- Subjects
- Humans, Infusion Pumps, Implantable, Infusions, Intravenous instrumentation, Time Factors, Analgesia, Patient-Controlled instrumentation
- Published
- 1995
- Full Text
- View/download PDF
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