arachis hypogaea fruit extract

General Material Information

Preferred name	arachis hypogaea fruit extract
Trivial Name	Peanut oil
Short Description	extract of the fruit of the peanut, arachis hypogaea l., fabaceae
CAS Number	8002-03-7
ECHA Number	232-296-4
FDA UNII	Search
Synonyms	extract of the fruit of the peanut, arachis hypogaea l., fabaceae lathyrus esquirolii fruit extract peanut extract Peanut oil Peanut oil or Groundnut oil Earthnut oil Katchung oil Groundnut oil Arachis oil Peanut oils Arachis hypogaea hypogaea seed oil Fats and Glyceridic oils, arachis Fats and Glyceridic oils, groundnut Fats and Glyceridic oils, peanut

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Literature & References

	arachis hypogaea fruit extract
Canada Domestic Sub. List:	8002-03-7
Pubchem (sid):	135321133

Publications by PubMed
Plant growth promotion and root colonization by EPS producing Enterobacter sp. RZS5 under heavy metal contaminated soil.
Measurement of strontium isotope ratio in nitric acid extract of peanut testa by ICP-Q-MS after removal of Rb by extraction with pure water.
Functional properties of peanut fractions on the growth of probiotics and foodborne bacterial pathogens.
Bioavailability of polyphenols from peanut skin extract associated with plasma lipid lowering function.
Detecting internal quality of peanuts during storage using electronic nose responses combined with physicochemical methods.
Preparation of A-type proanthocyanidin dimers from peanut skins and persimmon pulp and comparison of the antioxidant activity of A-type and B-type dimers.
Effect of peanut skin extract on chemical stability and sensory properties of salami during storage.
Peanut defensins: Novel allergens isolated from lipophilic peanut extract.
Adsorption of peanut (Arachis hypogaea, Leguminosae) proteins by activated charcoal.
The innate response to peanut extract in ovine afferent lymph and its correlation with allergen sensitisation.
Inhibition of the transcription factor c-Jun by the MAPK family, and not the NF-κB pathway, suggests that peanut extract has anti-inflammatory properties.
Comparative proteomic analysis and IgE binding properties of peanut seed and testa (skin).
Application of proanthocyanidins from peanut skins as a natural yeast inhibitory agent.
Enhancement of Alcohol Metabolism by Sprouted Peanut Extract in SD Rats.
Moving from peanut extract to peanut components: towards validation of component-resolved IgE tests.
Purification and properties of an alpha-amylase protein-inhibitor from Arachis hypogaea seeds.
Comparative study on chemical compositions and properties of protein isolates from mung bean, black bean and bambara groundnut.
Peanut varieties with reduced Ara h 1 content indicating no reduced allergenicity.
Development and validation of a (semi-)quantitative UHPLC-MS/MS method for the determination of 191 mycotoxins and other fungal metabolites in almonds, hazelnuts, peanuts and pistachios.
Screening natural antioxidants in peanut shell using DPPH-HPLC-DAD-TOF/MS methods.
Evaluation of hypolipidemic effects of peanut skin-derived polyphenols in rats on Western-diet.
Value-added processing of peanut skins: antioxidant capacity, total phenolics, and procyanidin content of spray-dried extracts.
Improvement of ethanol production using Saccharomyces cerevisiae by enhancement of biomass and nutrient supplementation.
Analysis of the effector activity of Ara h 2 and Ara h 6 by selective depletion from a crude peanut extract.
Effects of peanut-skin procyanidin A1 on degranulation of RBL-2H3 cells.
General food semiochemicals attract omnivorous German cockroaches, Blattella germanica.
Quantification of specific IgE to whole peanut extract and peanut components in prediction of peanut allergy.
Aqueous extract of peanut skin and its main constituent procyanidin A1 suppress serum IgE and IgG1 levels in mice-immunized with ovalbumin.
Effect of peanut tannin extracts on growth of Aspergillus parasiticus and aflatoxin production.
Diagnostic accuracy of specific IgE to components in diagnosing peanut allergy: a systematic review.
CD4+ cells proliferate after peanut-extract-specific and CD8+ cells proliferate after polyclonal stimulation of PBMC of children with atopic dermatitis.
Anaphylaxis to lemon soap: citrus seed and peanut allergen cross-reactivity.
Evaluation of aqueous Moringa seed extract as a seed treatment biofungicide for groundnuts.
Treatment of anaphylactic sensitivity to peanuts by immunotherapy with injections of aqueous peanut extract.
Intestinal absorption of luteolin from peanut hull extract is more efficient than that from individual pure luteolin.
Immunological analysis of allergenic cross-reactivity between peanut and tree nuts.
Processing can alter the properties of peanut extract preparations.
Combined normal-phase and reversed-phase liquid chromatography/ESI-MS as a tool to determine the molecular diversity of A-type procyanidins in peanut skins.
Functional analysis of cross-reactive immunoglobulin E antibodies: peanut-specific immunoglobulin E sensitizes basophils to tree nut allergens.
The natural history of peanut allergy.
Treatment with oleic acid reduces IgE binding to peanut and cashew allergens.
Characterization of volatile compounds contributing to naturally occurring fruity fermented flavor in peanuts.
Interlaboratory evaluation of two enzyme-linked immunosorbent assay kits for the detection of egg, milk, wheat, buckwheat, and peanut in foods.
LC-MS/MS multi-method for mycotoxins after single extraction, with validation data for peanut, pistachio, wheat, maize, cornflakes, raisins and figs.
Automated aflatoxin analysis of foods and animal feeds using immunoaffinity column clean-up and high-performance liquid chromatographic determination.
[Effects of soluble carbohydrates from several tropical foods (cassava, peanuts, coconut and papaya) on calcium utilization in the rat].
Immunoaffinity column cleanup with liquid chromatography using post-column bromination for determination of aflatoxins in peanut butter, pistachio paste, fig paste, and paprika powder: collaborative study.
Screening and quantitation of ochratoxin A in corn, peanuts, beans, rice, and cassava.
Skin exposure promotes a Th2-dependent sensitization to peanut allergens.
Gene expression changes in the mesenteric lymph nodes of rats after oral peanut extract exposure.
Peanut allergens alter intestinal barrier permeability and tight junction localisation in Caco-2 cell cultures.
Identification of Maillard reaction products on peanut allergens that influence binding to the receptor for advanced glycation end products.
Purification and cloning of two high molecular mass isoforms of peanut seed oleosin encoded by cDNAs of equal sizes.
Free amino acid determination in whole peanut seeds.
Objective eliciting doses of peanut-allergic adults and children can be combined for risk assessment purposes.
Lactobacillus casei Shirota does not decrease the food allergic response to peanut extract in Brown Norway rats.
Analysis of the composition of an immunoglobulin E reactive high molecular weight protein complex of peanut extract containing Ara h 1 and Ara h 3/4.
IgE recognition patterns in peanut allergy are age dependent: perspectives of the EuroPrevall study.
Analysis of pesticides in nuts by online reversed-phase liquid chromatography-gas chromatography using the through-oven transfer adsorption/desorption interface.
[Surveillance on contamination of total aflatoxins in corn, peanut, rice, walnut and pine nut in several areas in China].
Performance of broiler chicks fed on diets containing urea ammoniated neem (Azadirachta indica) kernel cake.
Polyclonal and clonal analysis of human CD4+ T-lymphocyte responses to nut extracts.
Extraction procedures for oilseeds and related high fat-low moisture products.
Rumen dry matter and crude protein degradability of extracted or untreated oilseeds and Leucaena leucocephala leaves.
Peanut allergy: lymphocyte response to peanut extract.
Double-blind experiments on the effect of a peanut extract on the bleeding incidence in 92 haemophiliacs.
Immunochemical and biological quantification of peanut extract.
[The action of peanut extract on the blood coagulation system].
Influence of peanut extract on bleeding time.
Standardization of RP-HPLC methods for the detection of the major peanut allergens Ara h 1, Ara h 2 and Ara h 3.
Expression of a codon-optimised recombinant Ara h 2.02 peanut allergen in Escherichia coli.
Selective ablation of mast cells or basophils reduces peanut-induced anaphylaxis in mice.
Effect of chemical modifications on allergenic potency of peanut proteins.
Peanut allergy is common among hazelnut-sensitized subjects but is not primarily the result of IgE cross-reactivity.
The steroidogenic enzyme Cyp11a1 is essential for development of peanut-induced intestinal anaphylaxis.
Oral administration of chitin and chitosan prevents peanut-induced anaphylaxis in a murine food allergy model.
Randomized trial of peanut consumption in infants at risk for peanut allergy.
Dietary Elimination of Soybean Components Enhances Allergic Immune Response to Peanuts in BALB/c Mice.
Heterogeneous responses and cross reactivity between the major peanut allergens Ara h 1, 2,3 and 6 in a mouse model for peanut allergy.
Component-resolved IgE profiles in Austrian patients with a convincing history of peanut allergy.
DHA-rich tuna oil effectively suppresses allergic symptoms in mice allergic to whey or peanut.
Maternal and postnatal dietary probiotic supplementation enhances splenic regulatory T helper cell population and reduces peanut allergen-induced hypersensitivity responses in mice.
Blockade of peanut allergy with a novel Ara h 2-Fcγ fusion protein in mice.
The fraction of exhaled nitric oxide improves prediction of clinical allergic reaction to peanut challenge in children.
Benefits and limitations of molecular diagnostics in peanut allergy: Part 14 of the series Molecular Allergology.
Cutaneous or respiratory exposures to peanut allergens in mice and their impacts on subsequent oral exposure.
Significance of para-esophageal lymph nodes in food or aeroallergen-induced iNKT cell-mediated experimental eosinophilic esophagitis.
Ara h 2 is the best predictor for peanut allergy in adults.
Aryl hydrocarbon receptor activation affects the dendritic cell phenotype and function during allergic sensitization.
Role of complement in a murine model of peanut-induced anaphylaxis.
Redefining the major peanut allergens.
The relevance of basophil allergen sensitivity testing to distinguish between severe and mild peanut-allergic children.
In silico prediction of Ara h 2 T cell epitopes in peanut-allergic children.
Ara h 2 and Ara h 6 have similar allergenic activity and are substantially redundant.
The CD28/CTLA-4-B7 signaling pathway is involved in both allergic sensitization and tolerance induction to orally administered peanut proteins.
IgE, but not IgG4, antibodies to Ara h 2 distinguish peanut allergy from asymptomatic peanut sensitization.
IL-7Rα and L-selectin, but not CD103 or CD34, are required for murine peanut-induced anaphylaxis.
Non-dioxin-like AhR ligands in a mouse peanut allergy model.
Prevention of oral food allergy sensitization via skin application of food allergen in a mouse model.
A novel immunoassay using recombinant allergens simplifies peanut allergy diagnosis.
Cutaneous lymphocyte antigen and α4β7 T-lymphocyte responses are associated with peanut allergy and tolerance in children.
Staphylococcal-derived superantigen enhances peanut induced Th2 responses in the skin.
The 2S albumin allergens of Arachis hypogaea, Ara h 2 and Ara h 6, are the major elicitors of anaphylaxis and can effectively desensitize peanut-allergic mice.
Elevated antigen-driven IL-9 responses are prominent in peanut allergic humans.
Influence of enzymatic hydrolysis on the allergenicity of roasted peanut protein extract.
Activation of the aryl hydrocarbon receptor suppresses sensitization in a mouse peanut allergy model.
Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases.
CD4(+) CD25(+) T regulatory cells do not transfer oral tolerance to peanut allergens in a mouse model of peanut allergy.
Identification of markers that distinguish IgE- from IgG-mediated anaphylaxis.
Passive transient transfer of peanut allergy by liver transplantation.
The role of intestinal dendritic cells subsets in the establishment of food allergy.
Peanut sensitization in a group of allergic Egyptian children.
Pepsin-digested peanut contains T-cell epitopes but no IgE epitopes.
Peanut allergy: Clinical and immunologic differences among patients from 3 different geographic regions.
Contribution of classic and alternative effector pathways in peanut-induced anaphylactic responses.
Evaluation of IgE antibodies to recombinant peanut allergens in patients with reported reactions to peanut.
CD4-blockade can induce protection from peanut-induced anaphylaxis.
Human basophils: a unique biological instrument to detect the allergenicity of food.
Enteric reovirus infection stimulates peanut-specific IgG2a responses in a mouse food allergy model.
IgE to peanut allergen components: relation to peanut symptoms and pollen sensitization in 8-year-olds.
Targeting Toll-like receptors on dendritic cells modifies the T(H)2 response to peanut allergens in vitro.
Allergy to peanut lipid transfer protein (LTP): frequency and cross-reactivity between peanut and peach LTP.
T cell responses to major peanut allergens in children with and without peanut allergy.
Quercetin effectively quells peanut-induced anaphylactic reactions in the peanut sensitized rats.
Lipid transfer protein (Ara h 9) as a new peanut allergen relevant for a Mediterranean allergic population.
Assessment of three human FcepsilonRI-transfected RBL cell-lines for identifying IgE induced degranulation utilizing peanut-allergic patient sera and peanut protein extract.
Effects of phytic acid on peanut allergens and allergenic properties of extracts.
Immunologic and clinical responses to parenteral immunotherapy in peanut anaphylaxis--a study using IgE and IgG4 immunoblot monitoring.
Serological characteristics of peanut allergy.
Poor biologic activity of cross-reactive IgE directed to carbohydrate determinants of glycoproteins.
Allergenicity of various peanut products as determined by RAST inhibition.
Basophil activation tests for the diagnosis of food allergy in children.
Soy immunotherapy for peanut-allergic mice: modulation of the peanut-allergic response.
A comparison study on allergen components between Korean (Arachis fastigiata Shinpung) and American peanut (Arachis hypogaea Runner).
Treatment of peanut allergy with rush immunotherapy.
Comparative nasal absorption of allergens in atopic and nonatopic subjects.
Effector activity of peanut allergens: a critical role for Ara h 2, Ara h 6, and their variants.
Peanuts can contribute to anaphylactic shock by activating complement.
Impairing oral tolerance promotes allergy and anaphylaxis: a new murine food allergy model.
Porcine IgE in the context of experimental food allergy: purification and isotype-specific antibodies.
Effects of pulsed UV-light on peanut allergens in extracts and liquid peanut butter.
Disruption of T-cell immunoglobulin and mucin domain molecule (TIM)-1/TIM4 interaction as a therapeutic strategy in a dendritic cell-induced peanut allergy model.
Early clinical predictors of remission of peanut allergy in children.
Purification and characterization of natural Ara h 8, the Bet v 1 homologous allergen from peanut, provides a novel isoform.
Contribution of Ara h 2 to peanut-specific, immunoglobulin E-mediated, cell activation.
CD4+CD25+ T cells regulate the intensity of hypersensitivity responses to peanut, but are not decisive in the induction of oral sensitization.
The peanut allergy epidemic: allergen molecular characterisation and prospects for specific therapy.
Peanut-lupine antibody cross-reactivity is not associated to cross-allergenicity in peanut-sensitized mouse strains.
The effect of the food matrix on in vivo immune responses to purified peanut allergens.
Isolation and characterization of natural Ara h 6: evidence for a further peanut allergen with putative clinical relevance based on resistance to pepsin digestion and heat.
Systemic and oral immunogenicity of hemagglutinin protein of rinderpest virus expressed by transgenic peanut plants in a mouse model.
Importance of early allergen contact for the development of a sustained immunoglobulin E response in a dog model.
Patients with anaphylaxis to pea can have peanut allergy caused by cross-reactive IgE to vicilin (Ara h 1).
Modulation of ovomucoid-specific oral tolerance in mice fed plant extracts containing lectins.
A neonatal swine model for peanut allergy.
Patient-tailored cloning of allergens by phage display: peanut (Arachis hypogaea) profilin, a food allergen derived from a rare mRNA.
Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology.
[Food allergy: identifying and characterizing peanut allergens with patient sera and monoclonal antibodies].
Identification and characterization of a second major peanut allergen, Ara h II, with use of the sera of patients with atopic dermatitis and positive peanut challenge.
Peanut sensitivity as a cause of burning mouth.
Anaphylaxis to peanuts: clinical correlation to skin tests.
A single oral sensitization to peanut without adjuvant leads to anaphylaxis in mice.
Patterns of immunoglobulin G responses to egg and peanut allergens are distinct: ovalbumin-specific immunoglobulin responses are ubiquitous, but peanut-specific immunoglobulin responses are up-regulated in peanut allergy.
Probiotics have a different immunomodulatory potential in vitro versus ex vivo upon oral administration in children with food allergy.
Human subjects without peanut allergy demonstrate T cell-dependent, TH2-biased, peanut-specific cytokine and chemokine responses independent of TH1 expression.
Predictive value of skin prick tests using recombinant allergens for diagnosis of peanut allergy.
Patterns of food allergen-specific cytokine production by T lymphocytes of children with multiple allergies.
In vitro effect of phenolic antioxidants on germination, growth and aflatoxin B accumulation by peanut Aspergillus section Flavi.
Double-blind placebo-controlled challenges for peanut allergy the efficiency of blinding procedures and the allergenic activity of peanut availability in the recipes.
Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy.
Development of an epitope-specific analytical tool for the major peanut allergen Ara h 2 using a high-density multiple-antigenic peptide strategy.
Mixed antibody and T cell responses to peanut and the peanut allergens Ara h 1, Ara h 2, Ara h 3 and Ara h 6 in an oral sensitization model.
Relevance of Ara h1, Ara h2 and Ara h3 in peanut-allergic patients, as determined by immunoglobulin E Western blotting, basophil-histamine release and intracutaneous testing: Ara h2 is the most important peanut allergen.
RBL cells expressing human Fc epsilon RI are a sensitive tool for exploring functional IgE-allergen interactions: studies with sera from peanut-sensitive patients.
A murine model of peanut anaphylaxis: T- and B-cell responses to a major peanut allergen mimic human responses.
Peanut oil in vitamin A and D preparations: reactions to skin test and manifestation of symptoms.
Application of an electrophoretic methodology for the identification of low molecular weight proteins in foods.
Food allergen (peanut)-specific TH2 clones generated from the peripheral blood of a patient with peanut allergy.
Peanut oil is not allergenic to peanut-sensitive individuals.

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PhysChem Properties

Material listed in food chemical codex	No
Specific gravity	@ 25 °C
Pounds per Gallon	6.74 to 6.823
Refractive Index	1.363 to 1.369 @ 20 °C
Flash Point TCC Value	16.11 °C TCC
Shelf life	36 months (or longer if stored properly.)
Storage notes	Store in cool, dry place in tightly sealed containers, protected from heat and light.

Organoleptic Properties

Odor Type: Nutty
peanut, creamy, oily, fatty, roasted, nutty, peanut roasted peanut
General comment	Peanut
Mosciano, Gerard P&F 24, No. 1, 13, (1999)	At 10.00 %. Peanut, creamy, oily with a fatty roasted nutty depth
Flavor Type: Nutty
peanut, oily, roasted, nutty, fatty, peanut roasted peanut
Mosciano, Gerard P&F 24, No. 1, 13, (1999)	At 50.00 ppm. Peanut, oily, light roasted nutty and fatty nuance

Occurrences

Safety Information

Safety information


Hazards identification

Classification of the substance or mixture
GHS Classification in accordance with 29 CFR 1910 (OSHA HCS)
None found.
GHS Label elements, including precautionary statements

Pictogram

Hazard statement(s)
None found.
Precautionary statement(s)
None found.
Oral/Parenteral Toxicity:
Not determined
Dermal Toxicity:
Not determined
Inhalation Toxicity:
Not determined

Safety in use information

Category:
flavoring agents
Recommendation for arachis hypogaea fruit extract usage levels up to:
	not for fragrance use.

Safety references

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EPA Substance Registry Services (TSCA):8002-03-7

EPA ACToR:Toxicology Data

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National Institute of Allergy and Infectious Diseases:Data

arachis hypogaea fruit extract

Chemidplus:0008002037

EPA/NOAA CAMEO:hazardous materials