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Steven M Musser - One of the best experts on this subject based on the ideXlab platform.
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confirmation of Peanut Protein using peptide markers in dark chocolate using liquid chromatography tandem mass spectrometry lc ms ms
Journal of Agricultural and Food Chemistry, 2006Co-Authors: Kevin Shefcheck, John H Callahan, Steven M MusserAbstract:Detection of peptides from the Peanut allergen Ara h 1 by liquid chromatography−mass spectrometry (LC-MS) was used to identify and estimate total Peanut Protein levels in dark chocolate. A comparison of enzymatic digestion subsequent to and following extraction of Ara h 1 from the food matrix revealed better limits of detection (LOD) for the pre-extraction digestion (20 ppm) than for the postextraction digestion (50 ppm). Evaluation of LC-MS instruments and scan modes showed the LOD could be further reduced to 10 ppm via a triple-quadrupole and multiple-reaction monitoring. Improvements in extraction techniques combined with an increase in the amount of chocolate extracted (1 g) improved the LOD to 2 ppm of Peanut Protein. This method provides an unambiguous means of confirming the presence of the Peanut Protein in foods using peptide markers from a major allergen, Ara h 1, and can easily be modified to detect other food allergens. Keywords: Peanut Protein; Ara h 1; dark chocolate; allergen
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confirmation of Peanut Protein using peptide markers in dark chocolate using liquid chromatography tandem mass spectrometry lc ms ms
Journal of Agricultural and Food Chemistry, 2006Co-Authors: Kevin Shefcheck, John H Callahan, Steven M MusserAbstract:Detection of peptides from the Peanut allergen Ara h 1 by liquid chromatography-mass spectrometry (LC-MS) was used to identify and estimate total Peanut Protein levels in dark chocolate. A comparison of enzymatic digestion subsequent to and following extraction of Ara h 1 from the food matrix revealed better limits of detection (LOD) for the pre-extraction digestion (20 ppm) than for the postextraction digestion (50 ppm). Evaluation of LC-MS instruments and scan modes showed the LOD could be further reduced to 10 ppm via a triple-quadrupole and multiple-reaction monitoring. Improvements in extraction techniques combined with an increase in the amount of chocolate extracted (1 g) improved the LOD to 2 ppm of Peanut Protein. This method provides an unambiguous means of confirming the presence of the Peanut Protein in foods using peptide markers from a major allergen, Ara h 1, and can easily be modified to detect other food allergens.
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confirmation of the allergenic Peanut Protein ara h 1 in a model food matrix using liquid chromatography tandem mass spectrometry lc ms ms
Journal of Agricultural and Food Chemistry, 2004Co-Authors: Kevin Shefcheck, Steven M MusserAbstract:Enzymatic digestion of total Protein along with liquid chromatography/tandem mass spectrometry (LC/MS/MS) was used to confirm the presence of a major Peanut allergen in food. Several peptides obtained from the enzymatic digestion of the most abundant Peanut allergen, Ara h 1, were identified as specific peptide biomarkers for Peanut Protein. Using ice cream as a model food matrix, a method was developed for the detection of the allergen peptide biomarkers. A key component of the method was the use of molecular mass cutoff filters to enrich the Ara h 1 in the Protein extracts. By applying the method to ice cream samples containing various levels of Peanut Protein, levels as low as 10 mg/kg of Ara h 1 could routinely be detected. This method provides an unambiguous means of confirming the presence of the Peanut allergen, Ara h 1, in foods and can easily be modified to detect other food allergens.
Qiang Wang - One of the best experts on this subject based on the ideXlab platform.
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High-moisture extrusion process of transglutaminase-modified Peanut Protein: Effect of transglutaminase on the mechanics of the process forming a fibrous structure
Food Hydrocolloids, 2021Co-Authors: Jinchuang Zhang, Chen Qiongling, Yujie Zhang, Qiang WangAbstract:Abstract At present, the quality of the Peanut Protein-based meat substitutes developed by high-moisture extrusion process still cannot fully meet the consumers’ requirements from the aspect of the fiber strength. In this study, the Peanut Protein was modified by the transglutaminase (TGase) and then extruded under a high moisture condition (55%). Effect of TGase on the mechanics of the process forming a fibrous structure were investigated. Results showed that during the high-moisture extrusion process, the TGase can improve the sensory properties by affecting the layered structure forming speed of Peanut Protein, but excessive TGase (more than 0.2%) would accelerate the cross-linking, which was not conducive to the rearrangement of Protein molecules and the improvement of the fibrous structure. In the extruder barrel, TGase can promote the unfolding, aggregating, and cross-linking of the disorderly arranged Protein molecular chains, and help to break the hydrogen bonds and disulfide bonds, but enhance the hydrophobic interactions. Moreover, the TGase made the arachin molecular chains more flexible, which was beneficial to the subsequent rearrangement. In the die, during the rearrangement of the Protein molecules, the addition of 0.1% or 0.2% TGase can promote to form new hydrogen bonds and disulfide bonds to stabilize the Protein conformation. From the cooling zone to the extrudate, the TGase was beneficial to the stretching of Protein molecular chains and would promote to synthesize the larger Protein subunits (66 kDa). Under the effect of TGase, the main forces maintaining the fibrous structure were converted into the hydrophobic interactions, hydrogen bonds, and disulfide bonds. At the same time, after modified by the TGase, the proportion of four Protein secondary structures was presented as β-sheet > α-helix > β-turn > random coil structure. Therefore, the mechanism of the process for forming a fibrous structure of Peanut Protein with different aggregation degree modified by TGase has been clarified, which will be helpful for improving the quality of Peanut Protein-based meat substitutes.
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high moisture extrusion of Peanut Protein carrageenan sodium alginate wheat starch mixtures effect of different exogenous polysaccharides on the process forming a fibrous structure
Food Hydrocolloids, 2020Co-Authors: Jinchuang Zhang, Li Liu, Yuanrong Jiang, Faisal Shah, Qiang WangAbstract:Abstract Of particular interest in this present work is to gain knowledge about the process forming the fibrous structure of Peanut Protein affected by carrageenan (CA), sodium alginate (SA), and wheat starch (WS), respectively. The multi-scale structure and physicochemical properties of exogenous polysaccharide modified-Peanut Protein powder (PPP) in the six extrusion zones were widely investigated to explain the process forming a fibrous structure. Results showed that 0.1% CA could significantly improve the tensile resistant force (about 1.92 kg), but it was not conducive to the fiber orientation. 0.1% SA could significantly improve the fibrous degree (up to about 1.24), springiness, and the tensile resistant force, but the hardness and chewiness increased significantly. The larger the amount of WS (0–8%), the lower the fibrous degree was, and the hardness and chewiness were both significantly reduced. Furthermore, 0.1% CA, 0.1% SA or 2% WS can protect the molecular chains of conarachin and arachin from the thermal transition. The selected exogenous polysaccharides, especially the 2% WS, can promote the aggregation of Protein molecules mainly by breaking the intramolecular disulfide bonds, enhancing the hydrophobic interactions and increasing the apparent viscosity to stabilize the newly formed conformation. The Protein subunit with a molecular weight of 22 kDa can be largely impacted by the exogenous polysaccharides due to the degradation of the subunits at 42 kDa and 39 kDa. Additionally, 2% WS can further promote the synthesis of Protein subunits with larger molecular weight (66 kDa). The three exogenous polysaccharides can promote the opening of the α-helix and gradually converting into the β-turn and random coil structure. When mixing the PPP with 0.1% CA, the four Protein secondary structures were present with β-sheet > α-helix > β-turn > random coil in the extrudate. While mixing the PPP with 0.1% SA or 2% WS, the order was β-sheet > β-turn > α-helix > random coil. This study has provided useful information for producing vegetable Protein-based meat substitutes with rich fibrous structure by adding the exogenous polysaccharides.
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converting Peanut Protein biomass waste into double green meat substitutes using a high moisture extrusion process a multiscale method to explore a process for forming a meat like fibrous structure
Journal of Agricultural and Food Chemistry, 2019Co-Authors: Jinchuang Zhang, Li Liu, Yuanrong Jiang, Shah Faisal, Linlin Wei, Chunjie Cao, Wenhui Yan, Qiang WangAbstract:Converting Peanut Protein biomass waste into environmentally friendly meat substitutes by a high-moisture extrusion process can help solve both resource and waste problems and be "double green". A multiscale method combined with some emerging techniques such as atomic force microscopy-based infrared spectroscopy and X-ray microscopy was used to make the whole extrusion process visible to show the process of forming a meat-like fibrous structure using two-dimensional and three-dimensional perspectives. The results showed that the Protein molecules underwent dramatic structural changes and unfolded in the extruder barrel, which created favorable conditions for molecular rearrangement in the subsequent zones. It was confirmed that the meat-like fibrous structure started to form at the junction of the die and the cooling zone and that this structure was caused by the phase separation and rearrangement of Protein molecules in the cooling zone. Moreover, the interactions between hydrogen bonds and disulfide bonds formed in the cooling zone maintained the meat-like fibrous structure with an α-helix > β-sheet > β-turn > random coil. Of the two main Peanut Proteins, arachin played a greater role in forming the fibrous structure than conarachin, especially those subunits of arachin with a molecular weight of 42, 39, and 22 kDa.
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high internal phase pickering emulsions stabilized solely by Peanut Protein isolate microgel particles with multiple potential applications
Angewandte Chemie, 2018Co-Authors: Bo Jiao, Qiang Wang, Aimin Shi, Bernard P BinksAbstract:High-internal-phase Pickering emulsions have various applications in materials science. However, the biocompatibility and biodegradability of inorganic or synthetic stabilizers limit their applications. Herein, we describe high-internal-phase Pickering emulsions with 87 % edible oil or 88 % n-hexane in water stabilized by Peanut-Protein-isolate microgel particles. These dispersed phase fractions are the highest in all known food-grade Pickering emulsions. The Protein-based microgel particles are in different aggregate states depending on the pH value. The emulsions can be utilized for multiple potential applications simply by changing the internal-phase composition. A substitute for partially hydrogenated vegetable oils is obtained when the internal phase is an edible oil. If the internal phase is n-hexane, the emulsion can be used as a template to produce porous materials, which are advantageous for tissue engineering.
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influence of extraction and solubilizing treatments on the molecular structure and functional properties of Peanut Protein
Lwt - Food Science and Technology, 2017Co-Authors: Hongguang Zhu, Qiang Wang, Jing Wang, Baoguo SunAbstract:Abstract As primary functional property of Protein in food industry, solubility was enhanced by various solubilization methods. Peanut Protein was used to prepare product with high solubility by physical and enzymatic hydrolysis methods. Effects of extraction and solubilizing treatments on Protein structure were evaluated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), scanning electron microscopy (SEM) and Fourier transform infrared spectroscopy (FT-IR). Changes of functional properties including emulsifying, water-holding, fat-binding, foaming and viscosity properties were observed and interpreted. Modification treatments which could improve the solubility were almost suitable for the promotion of emulsifying, fat-binding and foaming capacities, but not always suitable for the improvement of viscosity and water-holding properties. SDS-PAGE showed average molecular weight remained unaffected after physical modifications combined by high-speed stirring and ultrasonic treatment while reduced after limited enzymatic hydrolysis and high-pressure homogenization. The microstructure of Protein shown by SEM was gradually disbanded after all modification treatments. The regularity of Protein secondary structure, which was damaged during alcohol extraction, was reconstructed by combined physical modification and limited enzymatic hydrolysis. Depending on the demand of functional properties on final product, manufacture process could be optimized by the selection of modification treatments based on observing the changes in Protein structures.
Kevin Shefcheck - One of the best experts on this subject based on the ideXlab platform.
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confirmation of Peanut Protein using peptide markers in dark chocolate using liquid chromatography tandem mass spectrometry lc ms ms
Journal of Agricultural and Food Chemistry, 2006Co-Authors: Kevin Shefcheck, John H Callahan, Steven M MusserAbstract:Detection of peptides from the Peanut allergen Ara h 1 by liquid chromatography−mass spectrometry (LC-MS) was used to identify and estimate total Peanut Protein levels in dark chocolate. A comparison of enzymatic digestion subsequent to and following extraction of Ara h 1 from the food matrix revealed better limits of detection (LOD) for the pre-extraction digestion (20 ppm) than for the postextraction digestion (50 ppm). Evaluation of LC-MS instruments and scan modes showed the LOD could be further reduced to 10 ppm via a triple-quadrupole and multiple-reaction monitoring. Improvements in extraction techniques combined with an increase in the amount of chocolate extracted (1 g) improved the LOD to 2 ppm of Peanut Protein. This method provides an unambiguous means of confirming the presence of the Peanut Protein in foods using peptide markers from a major allergen, Ara h 1, and can easily be modified to detect other food allergens. Keywords: Peanut Protein; Ara h 1; dark chocolate; allergen
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confirmation of Peanut Protein using peptide markers in dark chocolate using liquid chromatography tandem mass spectrometry lc ms ms
Journal of Agricultural and Food Chemistry, 2006Co-Authors: Kevin Shefcheck, John H Callahan, Steven M MusserAbstract:Detection of peptides from the Peanut allergen Ara h 1 by liquid chromatography-mass spectrometry (LC-MS) was used to identify and estimate total Peanut Protein levels in dark chocolate. A comparison of enzymatic digestion subsequent to and following extraction of Ara h 1 from the food matrix revealed better limits of detection (LOD) for the pre-extraction digestion (20 ppm) than for the postextraction digestion (50 ppm). Evaluation of LC-MS instruments and scan modes showed the LOD could be further reduced to 10 ppm via a triple-quadrupole and multiple-reaction monitoring. Improvements in extraction techniques combined with an increase in the amount of chocolate extracted (1 g) improved the LOD to 2 ppm of Peanut Protein. This method provides an unambiguous means of confirming the presence of the Peanut Protein in foods using peptide markers from a major allergen, Ara h 1, and can easily be modified to detect other food allergens.
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confirmation of the allergenic Peanut Protein ara h 1 in a model food matrix using liquid chromatography tandem mass spectrometry lc ms ms
Journal of Agricultural and Food Chemistry, 2004Co-Authors: Kevin Shefcheck, Steven M MusserAbstract:Enzymatic digestion of total Protein along with liquid chromatography/tandem mass spectrometry (LC/MS/MS) was used to confirm the presence of a major Peanut allergen in food. Several peptides obtained from the enzymatic digestion of the most abundant Peanut allergen, Ara h 1, were identified as specific peptide biomarkers for Peanut Protein. Using ice cream as a model food matrix, a method was developed for the detection of the allergen peptide biomarkers. A key component of the method was the use of molecular mass cutoff filters to enrich the Ara h 1 in the Protein extracts. By applying the method to ice cream samples containing various levels of Peanut Protein, levels as low as 10 mg/kg of Ara h 1 could routinely be detected. This method provides an unambiguous means of confirming the presence of the Peanut allergen, Ara h 1, in foods and can easily be modified to detect other food allergens.
Jonathan Ob Hourihane - One of the best experts on this subject based on the ideXlab platform.
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continuous and daily oral immunotherapy for Peanut allergy results from a 2 year open label follow on study
The Journal of Allergy and Clinical Immunology: In Practice, 2020Co-Authors: Brian P. Vickery, Stacie M Jones, Wayne G Shreffler, Andrea Vereda, George Du Toit, Wesley A Burks, Katharina Blumchen, Caroline Nilsson, Montserrat Fernandezrivas, Jonathan Ob HourihaneAbstract:Background The randomized, controlled PALISADE trial demonstrated the benefit of daily oral immunotherapy with P eanu T (Arachis H ypogaea) allergen powder-dnfp (PTAH, formerly AR101) in Peanut-allergic children and adolescents. Objective ARC004, the open-label follow-on study to PALISADE, used 5 dosing cohorts to explore PTAH treatment beyond 1 year and alternative dosing regimens in Peanut-allergic individuals. Methods Active arm (PTAH-continuing) PALISADE participants who tolerated 300-mg Peanut Protein at the exit double-blind placebo-controlled food challenge and placebo arm (PTAH-naive) participants could enter ARC004. PTAH-continuing participants were assigned to receive daily (cohorts 1 and 3A) or non–daily (cohorts 2, 3B, and 3C) dosing regimens; PTAH-naive participants were built up to 300 mg/d PTAH, followed by maintenance dosing. At study completion, participants underwent an exit double-blind placebo-controlled food challenge with doses up to 2000 mg Peanut Protein. Data were assessed using descriptive statistics. Results Overall, 358 (87.5%) eligible participants (4-17 years) entered ARC004 (PTAH-continuing, n = 256; PTAH-naive, n = 102). Among PTAH-continuing participants, exposure-adjusted adverse event rates were 12.94 to 17.54/participant-year and 25.95 to 42.49/participant-year in daily and non–daily dosing cohorts, respectively; most participants (83%) experienced mild or moderate adverse events. Daily dosing cohorts appeared to have higher desensitization rates than non–daily dosing cohorts. Of all PTAH-continuing cohorts, cohort 3A had the longest daily dosing duration and the highest desensitization rates. Changes in immune markers with PTAH continuation demonstrated ongoing immunomodulation. Outcomes in PTAH-naive participants mirrored those of the PALISADE active arm. Conclusions Continued daily PTAH treatment beyond 1 year showed sustained safety and efficacy. Ongoing immunomodulation was observed during the second year of treatment.
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continuous and daily oral immunotherapy for Peanut allergy results from a 2 year open label follow on study
The Journal of Allergy and Clinical Immunology: In Practice, 2020Co-Authors: Brian P. Vickery, Stacie M Jones, Wayne G Shreffler, Andrea Vereda, George Du Toit, Wesley A Burks, Katharina Blumchen, Caroline Nilsson, Montserrat Fernandezrivas, Jonathan Ob HourihaneAbstract:ABSTRACT Background The randomized, controlled PALISADE trial demonstrated the benefit of daily oral immunotherapy with P eanu T ( A rachis H ypogaea) allergen powder-dnfp (PTAH, formerly AR101) in Peanut-allergic children and adolescents. Objective ARC004, the open-label follow-on study to PALISADE, used five dosing cohorts to explore PTAH treatment beyond 1 year and alternative dosing regimens in Peanut-allergic individuals. Methods Active arm (PTAH-continuing) PALISADE participants who tolerated 300-mg Peanut Protein at the exit double-blind placebo-controlled food challenge (DBPCFC) and placebo arm (PTAH-naive) participants could enter ARC004. PTAH-continuing participants were assigned to receive daily (Cohorts 1 and 3A) or non-daily (Cohorts 2, 3B, and 3C) dosing regimens; PTAH-naive participants were built up to 300-mg/day PTAH, followed by maintenance dosing. At study completion, participants underwent an exit DBPCFC with doses up to 2000-mg Peanut Protein. Data were assessed using descriptive statistics. Results Overall, 358 (87.5%) eligible participants (4-17 years) entered ARC004 (PTAH-continuing, n=256; PTAH-naive, n=102). Among PTAH-continuing participants, exposure-adjusted adverse event (AE) rates were 12.94-17.54/participant-year (PY) and 25.95-42.49/PY in daily and non-daily dosing cohorts, respectively; most participants (83%) experienced mild or moderate AEs. Daily dosing cohorts appeared to have higher desensitization rates than non-daily dosing cohorts. Of all PTAH-continuing cohorts, Cohort 3A had the longest daily dosing duration and the highest desensitization rates. Changes in immune markers with PTAH continuation demonstrated ongoing immunomodulation. Outcomes in PTAH-naive participants mirrored those of the PALISADE active arm. Conclusion Continued daily PTAH treatment beyond 1 year showed sustained safety and efficacy. Ongoing immunomodulation was observed during the second year of treatment.
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effect of epicutaneous immunotherapy vs placebo on reaction to Peanut Protein ingestion among children with Peanut allergy the pepites randomized clinical trial
JAMA, 2019Co-Authors: David Fleischer, Matthew Greenhawt, Kirsten Beyer, Gordon Sussman, Terri F Brownwhitehorn, Philippe Begin, Anna Nowakwegrzyn, Daniel Petroni, Jacques Hebert, Jonathan Ob HourihaneAbstract:Importance There are currently no approved treatments for Peanut allergy. Objective To assess the efficacy and adverse events of epicutaneous immunotherapy with a Peanut patch among Peanut-allergic children. Design, Setting, and Participants Phase 3, randomized, double-blind, placebo-controlled trial conducted at 31 sites in 5 countries between January 8, 2016, and August 18, 2017. Participants included Peanut-allergic children (aged 4-11 years [n = 356] without a history of a severe anaphylactic reaction) developing objective symptoms during a double-blind, placebo-controlled food challenge at an eliciting dose of 300 mg or less of Peanut Protein. Interventions Daily treatment with Peanut patch containing either 250 μg of Peanut Protein (n = 238) or placebo (n = 118) for 12 months. Main Outcomes and Measures The primary outcome was the percentage difference in responders between the Peanut patch and placebo patch based on eliciting dose (highest dose at which objective signs/symptoms of an immediate hypersensitivity reaction developed) determined by food challenges at baseline and month 12. Participants with baseline eliciting dose of 10 mg or less were responders if the posttreatment eliciting dose was 300 mg or more; participants with baseline eliciting dose greater than 10 to 300 mg were responders if the posttreatment eliciting dose was 1000 mg or more. A threshold of 15% or more on the lower bound of a 95% CI around responder rate difference was prespecified to determine a positive trial result. Adverse event evaluation included collection of treatment-emergent adverse events (TEAEs). Results Among 356 participants randomized (median age, 7 years; 61.2% male), 89.9% completed the trial; the mean treatment adherence was 98.5%. The responder rate was 35.3% with Peanut-patch treatment vs 13.6% with placebo (difference, 21.7% [95% CI, 12.4%-29.8%;P Conclusions and Relevance Among Peanut-allergic children aged 4 to 11 years, the percentage difference in responders at 12 months with the 250-μg Peanut-patch therapy vs placebo was 21.7% and was statistically significant, but did not meet the prespecified lower bound of the confidence interval criterion for a positive trial result. The clinical relevance of not meeting this lower bound of the confidence interval with respect to the treatment of Peanut-allergic children with epicutaneous immunotherapy remains to be determined. Trial Registration ClinicalTrials.gov Identifier:NCT02636699
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ar101 oral immunotherapy for Peanut allergy
The New England Journal of Medicine, 2018Co-Authors: Brian P. Vickery, Stacie M Jones, Jonathan Ob Hourihane, Kirsten Beyer, Wayne G Shreffler, Andrea Vereda, Thomas B Casale, George Du Toit, Annette MarcantonioAbstract:BACKGROUND Peanut allergy, for which there are no approved treatment options, affects patients who are at risk for unpredictable and occasionally life-threatening allergic reactions. METHODS In a phase 3 trial, we screened participants 4 to 55 years of age with Peanut allergy for allergic dose-limiting symptoms at a challenge dose of 100 mg or less of Peanut Protein (approximately one third of a Peanut kernel) in a double-blind, placebo-controlled food challenge. Participants with an allergic response were randomly assigned, in a 3:1 ratio, to receive AR101 (a Peanut-derived investigational biologic oral immunotherapy drug) or placebo in an escalating-dose program. Participants who completed the regimen (i.e., received 300 mg per day of the maintenance regimen for approximately 24 weeks) underwent a double-blind, placebo-controlled food challenge at trial exit. The primary efficacy end point was the proportion of participants 4 to 17 years of age who could ingest a challenge dose of 600 mg or more, without dose-limiting symptoms. RESULTS Of the 551 participants who received AR101 or placebo, 496 were 4 to 17 years of age; of these, 250 of 372 participants (67.2%) who received active treatment, as compared with 5 of 124 participants (4.0%) who received placebo, were able to ingest a dose of 600 mg or more of Peanut Protein, without dose-limiting symptoms, at the exit food challenge (difference, 63.2 percentage points; 95% confidence interval, 53.0 to 73.3; P<0.001). During the exit food challenge, the maximum severity of symptoms was moderate in 25% of the participants in the active-drug group and 59% of those in the placebo group and severe in 5% and 11%, respectively. Adverse events during the intervention period affected more than 95% of the participants 4 to 17 years of age. A total of 34.7% of the participants in the active-drug group had mild events, as compared with 50.0% of those in the placebo group; 59.7% and 44.4% of the participants, respectively, had events that were graded as moderate, and 4.3% and 0.8%, respectively, had events that were graded as severe. Efficacy was not shown in the participants 18 years of age or older. CONCLUSIONS In this phase 3 trial of oral immunotherapy in children and adolescents who were highly allergic to Peanut, treatment with AR101 resulted in higher doses of Peanut Protein that could be ingested without dose-limiting symptoms and in lower symptom severity during Peanut exposure at the exit food challenge than placebo. (Funded by Aimmune Therapeutics; PALISADE ClinicalTrials.gov number, NCT02635776 .).
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Peanut allergen threshold study pats novel single dose oral food challenge study to validate eliciting doses in children with Peanut allergy
The Journal of Allergy and Clinical Immunology, 2017Co-Authors: Jonathan Ob Hourihane, Julie A Nordlee, Wayne G Shreffler, Katrina J Allen, Gillian Dunngalvin, Giovanni A Zurzolo, Audrey Dunngalvin, Lyle C GurrinAbstract:Background Eliciting doses (EDs) of allergenic foods can be defined by the distribution of threshold doses for subjects within a specific population. The ED 05 is the dose that elicits a reaction in 5% of allergic subjects. The predicted ED 05 for Peanut is 1.5 mg of Peanut Protein (6 mg of whole Peanut). Objective We sought to validate the predicted Peanut ED 05 (1.5 mg) with a novel single-dose challenge. Methods Consecutive eligible children with Peanut allergy in 3 centers were prospectively invited to participate, irrespective of previous reaction severity. Predetermined criteria for objective reactions were used to identify ED 05 single-dose reactors. Results Five hundred eighteen children (mean age, 6.8 years) were eligible. No significant demographic or clinical differences were identified between 381 (74%) participants and 137 (26%) nonparticipants or between subjects recruited at each center. Three hundred seventy-eight children (206 male) completed the study. Almost half the group reported ignoring precautionary allergen labeling. Two hundred forty-five (65%) children experienced no reaction to the single dose of Peanut. Sixty-seven (18%) children reported a subjective reaction without objective findings. Fifty-eight (15%) children experienced signs of a mild and transient nature that did not meet the predetermined criteria. Only 8 (2.1%; 95% CI, 0.6%-3.4%) subjects met the predetermined criteria for an objective and likely related event. No child experienced more than a mild reaction, 4 of the 8 received oral antihistamines only, and none received epinephrine. Food allergy–related quality of life improved from baseline to 1 month after challenge regardless of outcome (η 2 = 0.2, P 05 . Conclusion A single administration of 1.5 mg of Peanut Protein elicited objective reactions in fewer than the predicted 5% of patients with Peanut allergy. The novel single-dose oral food challenge appears clinically safe and patient acceptable, regardless of the outcome. It identifies the most highly dose-sensitive population with food allergy not otherwise identifiable by using routinely available Peanut skin prick test responses or specific IgE levels, but this single-dose approach has not yet been validated for risk assessment of individual patients.
Mouming Zhao - One of the best experts on this subject based on the ideXlab platform.
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the umami intensity enhancement of Peanut Protein isolate hydrolysate and its derived factions and peptides by maillard reaction and the analysis of peptide ep maillard products
Food Research International, 2019Co-Authors: Jianan Zhang, Mouming Zhao, Dongxiao Sunwaterhouse, Yunzi Feng, Lianzhu LinAbstract:Abstract This study aimed to examine the feasibility of improving umami taste of Peanut Protein isolate hydrolysate (PPIH) and its fractions (obtained via ethanol precipitation and gel filtration chromatography) and peptide constituents, through their reactions with glucose at 98 °C for 70 min (Maillard reaction). To get insights into the characteristics of the peptide contributors with high umami intensity and/or umami-enhancing activity, Maillard reaction-guided and sensory-guided fractionation and characterization using ultra-performance liquid chromatography tandem mass spectrometry (UPLC-MS/MS) and eXpose algorithm calculation method were subsequently involved. Three umami and umami-enhancing peptides, three umami-enhancing peptides with other tastes, three bitter peptides and one astringent peptide were found. For the first time, peptide TP was reported to suppress umami intensity of monosodium glutamate (MSG) aqueous solution. Combined treatments of enzymatic hydrolysis and Maillard reaction on PPI facilitated umami enhancement. Maillard products of identified peptides had higher umami intensities and/or greater umami-enhancing abilities. Pyroglutamylproline (pyroEP) and glucosylated EP were discovered as the major compounds of EP Maillard product.
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identification and taste characteristics of novel umami and umami enhancing peptides separated from Peanut Protein isolate hydrolysate by consecutive chromatography and uplc esi qtof ms ms
Food Chemistry, 2019Co-Authors: Jianan Zhang, Mouming Zhao, Lianzhu LinAbstract:Abstract Six novel peptides were separated from Peanut Protein isolate hydrolysate (PPIH) using ethanol precipitation and gel chromatography, and identified as DQR, NNP, EGF, EDG, TESSSE and RGENESEEEGAIVT by UPLC–ESI–QTOF–MS/MS. On the basis of sensory results, all peptides were perceived umami with threshold values from 0.39 to 1.11 mM and had umami-enhancing abilities simultaneously with threshold values from 0.33 to 0.82 mM. RGENESEEEGAIVT was the first discovered tetradecapeptide with umami and umami-enhancing ability. The dose–response test revealed that umami-enhancing activities of identified peptides were different: TESSSE and RGENESEEEGAIVT imparted better umami intensity when equimolar monosodium glutamate (MSG) was added into 0.5 g/L MSG solution. Taste profile analyses of complex mixtures with/without synthetic peptides were determined by both electronic tongue and human panellists, suggesting that umami peptides influence multiple tastes and electronic tongue has the potential to replace sensory test to distinguish taste attributes of foods rich in peptides.
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emulsification performance and interfacial properties of enzymically hydrolyzed Peanut Protein isolate pretreated by extrusion cooking
Food Hydrocolloids, 2017Co-Authors: Lin Chen, Jianshe Chen, Mouming ZhaoAbstract:Abstract In this study, Peanut Protein isolate (PPI) was modified with extrusion pretreatment and papain-induced proteolysis. SDS-polyacrylamide gel electrophoresis showed that extrusion pretreatment conducted at 130 °C substantially increased the protease accessibilities of the major constitutive Proteins (conarachin and arachin) in EPPI (extrudates of PPI), resulting in a remarkable increase in the degree of hydrolysis (DH) and Protein solubility for the hydrolysates. Analysis of droplet size distributions and microstructures of oil-in-water model emulsions formed by PPIH (PPI hydrolysates) and EPPIH (EPPI hydrolysates) with different DH showed that extrusion pretreatment led to a marked enhancement in the emulsification performance for the hydrolysates. EPPIH (6.2% DH) was capable of producing a stable emulsion (20 vol% sunflower seed oil) with fine droplets ( d 32 = 0.4 μ m, d 43 = 1.6 μ m) at 2.5% (w/v) sample content, whilst the equivalent emulsions made with control PPI and PPIH (0.9% DH) required 6.5% and 5.5% (w/v) level of sample, respectively. Based on investigations of surface pressure versus sample concentration profiles and saturation surface Loads ( Γ sat ) for some selected PPIH and EPPIH, it was found that with most insoluble Protein particles in EPPIH being enzymically hydrolyzed and becoming soluble, the production of surface active peptides with low Γ sat was substantially promoted during enzymic proteolysis, which was responsible for the efficient use of EPPIH (6.2% DH) on generating and stabilizing small emulsion droplets against bridging flocculation during homogenization. These results indicated that hydrolyzed PPI could be used an efficient food emulsifying agent with extrusion pretreatment substantially increasing its protease accessibility.
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mechanism of the discrepancy in the enzymatic hydrolysis efficiency between defatted Peanut flour and Peanut Protein isolate by flavorzyme
Food Chemistry, 2015Co-Authors: Lin Zheng, Yijun Zhao, Chuqiao Xiao, Dongxiao Sunwaterhouse, Mouming ZhaoAbstract:Both defatted Peanut flour (DPF) and Peanut Protein isolate (PPI) are widely used to prepare Peanut Protein hydrolysates. To compare their enzymatic hydrolysis efficiencies, DPF and PPI were hydrolysed by Alcalase, Neutrase, Papain, Protamex and Flavorzyme. Alcalase and Flavorzyme were found to be the most efficient proteases to hydrolyse both DPF and PPI. The efficiency was comparable to each other when using Alcalase, while PPI was hydrolysed less efficiently than DPF when using Flavorzyme. Analysis of changes in the Protein solubility, subunit and conformation, and amino acid composition of DPF, PPI and their Flavorzyme hydrolysis residues indicated that the PPI preparation process had minimal effect on it, but peptide aggregation via non-covalent bonding (including hydrophobic interactions and hydrogen bonds) during hydrolysis and/or thermal treatment after hydrolysis were likely responsible for the reduced hydrolysis efficiency of PPI by Flavorzyme.
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improvement of functional properties of Peanut Protein isolate by conjugation with dextran through maillard reaction
Food Chemistry, 2012Co-Authors: Yan Liu, Mouming Zhao, Guanli Zhao, Jiaoyan Ren, Bao YangAbstract:Reaction mixtures containing Peanut Protein isolate (PPI) and dextran (1:1 weight ratio) were dry-heated at 60 °C and 79% relative humidity for 7 days. SDS–PAGE analysis indicated that PPI had become complexed with dextran to form conjugates of higher molecular weight. Arachin, accounting for 50% of Peanut Proteins, was hard to glycosylate with dextran, which might limit the extent of glycosylation of PPI. The thermal stability of PPI was remarkably improved by mixture/conjugation with dextran. Proteins in mixtures/conjugates might have a more compacted tertiary conformation than PPI. The Protein solubility of conjugates at pH 4.5–6.0 was remarkably increased compared with the PPI/mixture. Mixture with dextran could significantly improve the emulsifying and foaming properties of PPI (p < 0.05). Conjugation with dextran could further enhance emulsifying and foaming properties of PPI.