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Mongkhon Sompornrattanaphan - One of the best experts on this subject based on the ideXlab platform.
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omega 5 and gamma gliadin are the major allergens in adult onset ige mediated wheat allergy results from thai cohort with oral food challenge
Journal of Asthma and Allergy, 2021Co-Authors: Surapon Piboonpocanun, Punchama Pacharn, Torpong Thongngarm, Chamard Wongsa, Onrapak Reamtong, Mongkhon SompornrattanaphanAbstract:Background Various clinical patterns based on routes of sensitization and sensitized allergens are reported in adult-onset IgE-mediated wheat allergy. There is still a paucity of data on IgE-bound wheat allergen profiles in wheat challenge-proven adult-onset wheat allergic cases. Therefore, we aim to identify the major sensitized allergens in Thai adult-onset wheat allergic patients whose first symptom occurred after the age of 18 years despite previous tolerance. Methods This cross-sectional pilot study recruited patients from the Thai Adult-onset IgE-mediated Wheat Allergy Cohort (TAWAC). The sera of patients with mostly challenge-proven cases were selected for allergen study, including ImmunoCAP and IgE-bound gliadins along with Glutenins profiles. The IgE-bound proteins were identified by liquid chromatography-tandem mass spectrophotometry (LC-MS/MS). Direct binding of IgE to recombinant gliadin and glutenin was performed to confirm the results of immunoblot and LC-MS/MS. Results Eleven wheat-dependent exercise-induced anaphylaxis (WDEIA) and 4 typical wheat allergy (WA) patients were enrolled. Serum IgE from >50% of bound proteins had a molecular weight ranging from 35 to 55 kDa in both gliadin and glutenin extracts. Further, ELISA demonstrated that γ-gliadin and ω5-gliadin were the most important major allergens. Other major allergens include α/β-gliadin, HMW glutenin, and possibly α-amylase inhibitor or LWM glutenin. Gamma-gliadin sensitization was found in all WA patients (4/4), while ω-5 gliadin was found in all WDEIA patients (11/11) from ELISA. Conclusion Wheat γ-gliadin and ω-5 gliadin are major wheat allergens among adult-onset wheat allergy patients in Thailand. Component-resolved diagnosis using γ-gliadin might be helpful in high suspicion of wheat allergy.
Surapon Piboonpocanun - One of the best experts on this subject based on the ideXlab platform.
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omega 5 and gamma gliadin are the major allergens in adult onset ige mediated wheat allergy results from thai cohort with oral food challenge
Journal of Asthma and Allergy, 2021Co-Authors: Surapon Piboonpocanun, Punchama Pacharn, Torpong Thongngarm, Chamard Wongsa, Onrapak Reamtong, Mongkhon SompornrattanaphanAbstract:Background Various clinical patterns based on routes of sensitization and sensitized allergens are reported in adult-onset IgE-mediated wheat allergy. There is still a paucity of data on IgE-bound wheat allergen profiles in wheat challenge-proven adult-onset wheat allergic cases. Therefore, we aim to identify the major sensitized allergens in Thai adult-onset wheat allergic patients whose first symptom occurred after the age of 18 years despite previous tolerance. Methods This cross-sectional pilot study recruited patients from the Thai Adult-onset IgE-mediated Wheat Allergy Cohort (TAWAC). The sera of patients with mostly challenge-proven cases were selected for allergen study, including ImmunoCAP and IgE-bound gliadins along with Glutenins profiles. The IgE-bound proteins were identified by liquid chromatography-tandem mass spectrophotometry (LC-MS/MS). Direct binding of IgE to recombinant gliadin and glutenin was performed to confirm the results of immunoblot and LC-MS/MS. Results Eleven wheat-dependent exercise-induced anaphylaxis (WDEIA) and 4 typical wheat allergy (WA) patients were enrolled. Serum IgE from >50% of bound proteins had a molecular weight ranging from 35 to 55 kDa in both gliadin and glutenin extracts. Further, ELISA demonstrated that γ-gliadin and ω5-gliadin were the most important major allergens. Other major allergens include α/β-gliadin, HMW glutenin, and possibly α-amylase inhibitor or LWM glutenin. Gamma-gliadin sensitization was found in all WA patients (4/4), while ω-5 gliadin was found in all WDEIA patients (11/11) from ELISA. Conclusion Wheat γ-gliadin and ω-5 gliadin are major wheat allergens among adult-onset wheat allergy patients in Thailand. Component-resolved diagnosis using γ-gliadin might be helpful in high suspicion of wheat allergy.
Peter Koehler - One of the best experts on this subject based on the ideXlab platform.
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Comparative Study on Gluten Protein Composition of Ancient (Einkorn, Emmer and Spelt) and Modern Wheat Species (Durum and Common Wheat)
Foods (Basel Switzerland), 2019Co-Authors: Sabrina Geisslitz, Katharina Anne Scherf, C. Friedrich H. Longin, Peter KoehlerAbstract:The spectrophotometric Bradford assay was adapted for the analysis of gluten protein contents (gliadins and Glutenins) of spelt, durum wheat, emmer and einkorn. The assay was applied to a set of 300 samples, including 15 cultivars each of common wheat, spelt, durum wheat, emmer and einkorn cultivated at four locations in Germany in the same year. The total protein content was equally influenced by location and wheat species, however, gliadin, glutenin and gluten contents were influenced more strongly by wheat species than location. Einkorn, emmer and spelt had higher protein and gluten contents than common wheat at all four locations. However, common wheat had higher glutenin contents than einkorn, emmer and spelt resulting in increasing ratios of gliadins to Glutenins from common wheat (< 3.8) to spelt, emmer and einkorn (up to 12.1). With the knowledge that glutenin contents are suitable predictors for high baking volume, cultivars of einkorn, emmer and spelt with good predicted baking performance were identified. Finally, spelt, emmer and einkorn were found to have a higher nitrogen partial factor productivity than common and durum wheat making them promising crops for a more sustainable agriculture.
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gluten protein composition and aggregation properties as predictors for bread volume of common wheat spelt durum wheat emmer and einkorn
Journal of Cereal Science, 2018Co-Authors: Sabrina Geisslitz, Katharina Anne Scherf, Peter KoehlerAbstract:Abstract The technological properties of the ancient wheat species spelt, emmer and einkorn are considered inferior compared to common wheat and durum wheat, but there are only few comparative studies between ancient and modern wheat species. To help fill this gap, protein content and composition, gluten aggregation, dough and bread properties were determined in a unique set of eight cultivars each of common wheat, spelt, durum wheat, emmer and einkorn grown under standardized conditions at one location in the same year. Spearman correlations and principal component analysis (PCA) revealed that especially the contents of Glutenins, high-molecular-weight glutenin subunits and glutenin macropolymer were suitable to predict the volume of breads made from wholemeal flours of the five wheat species using microbaking tests. Based on their proximity to common wheat in the PCA, one cultivar each of spelt, emmer and einkorn was identified that had similar protein analytical, functional and baking properties to common wheat. Furthermore, the characterization of gluten aggregation behavior using the GlutoPeak test (GPT) enabled an estimation of dough properties and bread volume. Therefore, the fast and easy GPT may serve as an alternative to time-consuming and labor-intensive baking tests.
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SDS-PAGE of flours, prolamin and glutelin fractions and isolated gluten protein types.
2017Co-Authors: Kathrin Schalk, Peter Koehler, Barbara Lexhaller, Katharina Anne ScherfAbstract:(A) Wheat. M: marker, 1: wheat flour, 2: wheat prolamin fraction, 3: ω5-gliadins, 4: ω1,2-gliadins, 5: α-gliadins, 6: γ-gliadins, 7: wheat glutelin fraction, 8: high-molecular-weight glutenin subunits (HMW-GS), 9: low-molecular-weight glutenin subunits (LMW-GS). (B) Rye. M: marker, 10: rye flour, 11: rye prolamin fraction, 12: ω-secalins, 13: γ-75k-secalins, 14: γ-40k-secalins, 15: rye glutelin fraction, 16: HMW-secalins. (C) Barley. M: marker, 17: barley flour, 18: barley prolamin fraction, 19: γ/B-hordeins, 20: C-hordeins, 21: barley glutelins, 22: B/γ-hordeins, 23: D-hordeins. (D) Oats. 24: oat prolamin fraction (avenins), 25: oat flour.
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improved quantitation of gluten in wheat starch for celiac disease patients by gel permeation high performance liquid chromatography with fluorescence detection gp hplc fld
Journal of Agricultural and Food Chemistry, 2016Co-Authors: Katharina Anne Scherf, Peter KoehlerAbstract:Purified wheat starch (WSt) is commonly used in gluten-free products for celiac disease (CD) patients. It is mostly well-tolerated, but doubts about its safety for CD patients persist. One reason may be that most ELISA kits primarily recognize the alcohol-soluble gliadin fraction of gluten, but insufficiently target the alcohol-insoluble glutenin fraction. To address this problem, a new sensitive method based on the sequential extraction of gliadins, Glutenins, and gluten from WSt followed by gel-permeation high-performance liquid chromatography with fluorescence detection (GP-HPLC-FLD) was developed. It revealed that considerable amounts of Glutenins were present in most WSt. The gluten contents quantitated by GP-HPLC-FLD as sum of gliadins and Glutenins were higher than those by R5 ELISA (gluten as gliadin content multiplied by a factor of 2) in 19 out of 26 WSt. Despite its limited selectivity, GP-HPLC-FLD may be applied as confirmatory method to ELISA to quantitate gluten in WSt.
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split nitrogen application improves wheat baking quality by influencing protein composition rather than concentration
Frontiers in Plant Science, 2016Co-Authors: Peter Koehler, Cheng Xue, Gunda Schulte Aufm Erley, Anne Rossmann, Ramona Schuster, Karlhermann MuhlingAbstract:The use of late nitrogen (N) fertilization (N application at late growth stages of wheat, e.g. booting, heading or anthesis) to improve baking quality of wheat has been questioned. Although it increases protein concentration, the beneficial effect on baking quality (bread loaf volume) needs to be clearly understood. Two pot experiments were conducted aiming to evaluate whether late N is effective under controlled conditions and if these effects result from increased N rate or N splitting. Late N fertilizers were applied either as additional N or split from the basal N at late boot stage or heading in the form of nitrate-N or urea. Results showed that late N fertilization improved loaf volume of wheat flour by increasing grain protein concentration and altering its composition. Increasing N rate mainly enhanced grain protein quantitatively. However, N splitting changed grain protein composition by enhancing the percentages of gliadins and Glutenins as well as certain high molecular weight glutenin subunits (HMW-GS), which led to an improved baking quality of wheat flour. The late N effects were greater when applied as nitrate-N than urea. The proportions of glutenin and x-type HMW-GS were more important than the overall protein concentration in determining baking quality. N splitting is more effective in improving wheat quality than the increase in the N rate by late N, which offers the potential to cut down N fertilization rates in wheat production systems.
Xu Jia - One of the best experts on this subject based on the ideXlab platform.
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Deletion of high-molecular-weight glutenin subunits in wheat significantly reduced dough strength and bread-baking quality
BMC plant biology, 2018Co-Authors: Yingjun Zhang, Qian Liu, Lijing Sun, Xiyong Chen, Yuping Liu, Xu JiaAbstract:High-molecular-weight glutenin subunits (HMW-GS) play important roles in the elasticity of dough made from wheat. The HMW-GS null line is useful for studying the contribution of HMW-GS to the end-use quality of wheat. In a previous work, we cloned the Glu-1Ebx gene from Thinopyrum bessarabicum and introduced it into the wheat cultivar, Bobwhite. In addition to lines expressing the Glu-1Ebx gene, we also obtained a transgenic line (LH-11) with all the HMW-GS genes silenced. The HMW-GS deletion was stably inherited as a dominant and conformed to Mendel’s laws. Expression levels of HMW-GS were determined by RT-PCR and epigenetic changes in methylation patterns and small RNAs were analyzed. Glutenins and gliadins were separated and quantitated by reversed-phase ultra-performance liquid chromatography. Measurement of glutenin macropolymer, and analysis of agronomic traits and end-use quality were also performed. DNA methylation and the presence of small double-stranded RNA may be the causes of post-transcriptional gene silencing in LH-11. The accumulation rate and final content of glutenin macropolymer (GMP) in LH-11 were significantly lower than in wild-type (WT) Bobwhite. The total protein content was not significantly affected as the total gliadin content increased in LH-11 compared to WT. Deletion of HMW-GS also changed the content of different gliadin fractions. The ratio of ω-gliadin increased, whereas α/β- and γ-gliadins declined in LH-11. The wet gluten content, sedimentation value, development time and stability time of LH-11 were remarkably lower than that of Bobwhite. Bread cannot be made using the flour of LH-11. Post-transcriptional gene silencing through epigenetic changes and RNA inhibition appear to be the causes for the gene expression deficiency in the transgenic line LH-11. The silencing of HMW-GW in LH-11 significantly reduced the dough properties, GMP content, wet gluten content, sedimentation value, development time and stability time of flour made from this wheat cultivar. The HMW-GS null line may provide a potential material for biscuit-making because of its low dough strength.
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Deletion of high-molecular-weight glutenin subunits in wheat significantly reduced dough strength and bread-baking quality
BMC, 2018Co-Authors: Yingjun Zhang, Qian Liu, Lijing Sun, Xiyong Chen, Yuping Liu, Xu JiaAbstract:Abstract Background High-molecular-weight glutenin subunits (HMW-GS) play important roles in the elasticity of dough made from wheat. The HMW-GS null line is useful for studying the contribution of HMW-GS to the end-use quality of wheat. Methods In a previous work, we cloned the Glu-1E b x gene from Thinopyrum bessarabicum and introduced it into the wheat cultivar, Bobwhite. In addition to lines expressing the Glu-1E b x gene, we also obtained a transgenic line (LH-11) with all the HMW-GS genes silenced. The HMW-GS deletion was stably inherited as a dominant and conformed to Mendel’s laws. Expression levels of HMW-GS were determined by RT-PCR and epigenetic changes in methylation patterns and small RNAs were analyzed. Glutenins and gliadins were separated and quantitated by reversed-phase ultra-performance liquid chromatography. Measurement of glutenin macropolymer, and analysis of agronomic traits and end-use quality were also performed. Results DNA methylation and the presence of small double-stranded RNA may be the causes of post-transcriptional gene silencing in LH-11. The accumulation rate and final content of glutenin macropolymer (GMP) in LH-11 were significantly lower than in wild-type (WT) Bobwhite. The total protein content was not significantly affected as the total gliadin content increased in LH-11 compared to WT. Deletion of HMW-GS also changed the content of different gliadin fractions. The ratio of ω-gliadin increased, whereas α/β- and γ-gliadins declined in LH-11. The wet gluten content, sedimentation value, development time and stability time of LH-11 were remarkably lower than that of Bobwhite. Bread cannot be made using the flour of LH-11. Conclusions Post-transcriptional gene silencing through epigenetic changes and RNA inhibition appear to be the causes for the gene expression deficiency in the transgenic line LH-11. The silencing of HMW-GW in LH-11 significantly reduced the dough properties, GMP content, wet gluten content, sedimentation value, development time and stability time of flour made from this wheat cultivar. The HMW-GS null line may provide a potential material for biscuit-making because of its low dough strength
Onrapak Reamtong - One of the best experts on this subject based on the ideXlab platform.
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omega 5 and gamma gliadin are the major allergens in adult onset ige mediated wheat allergy results from thai cohort with oral food challenge
Journal of Asthma and Allergy, 2021Co-Authors: Surapon Piboonpocanun, Punchama Pacharn, Torpong Thongngarm, Chamard Wongsa, Onrapak Reamtong, Mongkhon SompornrattanaphanAbstract:Background Various clinical patterns based on routes of sensitization and sensitized allergens are reported in adult-onset IgE-mediated wheat allergy. There is still a paucity of data on IgE-bound wheat allergen profiles in wheat challenge-proven adult-onset wheat allergic cases. Therefore, we aim to identify the major sensitized allergens in Thai adult-onset wheat allergic patients whose first symptom occurred after the age of 18 years despite previous tolerance. Methods This cross-sectional pilot study recruited patients from the Thai Adult-onset IgE-mediated Wheat Allergy Cohort (TAWAC). The sera of patients with mostly challenge-proven cases were selected for allergen study, including ImmunoCAP and IgE-bound gliadins along with Glutenins profiles. The IgE-bound proteins were identified by liquid chromatography-tandem mass spectrophotometry (LC-MS/MS). Direct binding of IgE to recombinant gliadin and glutenin was performed to confirm the results of immunoblot and LC-MS/MS. Results Eleven wheat-dependent exercise-induced anaphylaxis (WDEIA) and 4 typical wheat allergy (WA) patients were enrolled. Serum IgE from >50% of bound proteins had a molecular weight ranging from 35 to 55 kDa in both gliadin and glutenin extracts. Further, ELISA demonstrated that γ-gliadin and ω5-gliadin were the most important major allergens. Other major allergens include α/β-gliadin, HMW glutenin, and possibly α-amylase inhibitor or LWM glutenin. Gamma-gliadin sensitization was found in all WA patients (4/4), while ω-5 gliadin was found in all WDEIA patients (11/11) from ELISA. Conclusion Wheat γ-gliadin and ω-5 gliadin are major wheat allergens among adult-onset wheat allergy patients in Thailand. Component-resolved diagnosis using γ-gliadin might be helpful in high suspicion of wheat allergy.