I would suggest this. Is it gluten intolerance, or are we adding an ingredient in the United States that is causing our digestive issues? My problem started 1 year ago. I feel very fortunate to have found that it isn't actually the gluten. It is the carcinogen "bromate". When I eat any wheat product that does not have bromate in it, I have no reaction. This carcinogen is not allowed in many countries including China???? The problem is that it is not required as a listed ingredient. Some of the places that I have found that do not use flour with bromate are Great Harvest Bread, and Panera Bread. I would suggest trying this. Then research, research, research. I buy pasta made in Italy, and make my own bakery items as much as possible. King Arthur flour is one of the brands that is not processed with Bromate. This epidemic is actually a poisoning. Is there any way to stop this???
Another Reason to Eat Organic – No Potassium Bromate in Your Bread
The gluten proteins gliadin and glutenin are important for dough and bread characteristics. In the present work, redox agents were used to impact gluten properties and to study gliadin-glutenin interactions in bread making. In control bread making, mixing increased the extractability of glutenin. The level of SDS-extractable glutenin decreased during fermentation and then further in the oven. The levels of extractable alpha- and gamma-gliadin also decreased during bread baking due to gliadin-glutenin polymerization. Neither oxidizing nor reducing agents had an impact on glutenin extractabilities after mixing. The redox additives did not affect omega-gliadin extractabilities during bread making due to their lack of cysteine residues. Potassium iodate (0.82-2.47 micromol/g of protein) and potassium bromate (1.07-3.17 micromol/g of protein) increased both alpha- and gamma-gliadin extractabilities during baking. Increasing concentrations of glutathione (1.15-3.45 micromol/g of protein) decreased levels of extractable alpha- and gamma-gliadins during baking. The work not only demonstrated that, during baking, glutenin and gliadin polymerize through heat-induced sulfhydryl-disulfide exchange reactions, but also demonstrated for the first time that oxidizing agents, besides their effect on dough rheology and hence bread volume, hinder gliadin-glutenin linking during baking, while glutathione increases the degree of covalent gliadin to glutenin linking.
Wheat proteins have been associated with a number of dietary disorders. The best well-known disorder is celiac disease, a disorder that develops in genetically susceptible individuals after ingesting gluten-containing cereals. Wheat gliadins, and to a lesser extent low molecular weight glutenins, carry immunogenic peptides . A variety of these celiac-disease-initiating peptides of α-gliadin have been identified. Examples of some of these immunogenic epitopes are glia-α9 (PFPQPQLPY) and glia-α20 (FRPQQPUPQ) . The unusual amino acid composition (high proline and glutamine contents) in gluten proteins prevents the complete digestion of these proteins in the gastrointestinal tract. While for most people the peptides do not cause any problems, an estimated 1% of the world population suffers from celiac disease  and in these individuals, these peptides trigger a cascade of auto-immune reactions that lead to severe intestinal damage. Several researchers have been trying to develop solutions for people suffering from celiac disease. One of these investigated solutions involves the pretreatment of the gluten protein with peptidase mixtures (e.g., papaya non-specific endopeptidase and three microbial peptidases (Aspergillus oryzae leucine aminopeptidase, Aspergillus melleus endopeptidase with activity against hydrophibic amino acid residues and Penicillium citrinum deutorlysin)) . These peptidases are able to digest the above proline-rich peptides and, hence lower the concentration of the immunogenic peptides. Other strategies include the development of wheat varieties that do not trigger these gastrointestinal responses  and targeted processing of the cereals. One of such novel cereals is tritordeum, a hybrid of durum wheat and wild barley . Tritordeum was shown to have lower numbers of immunogenic epitopes than regular wheat. This novel cereal is suitable to include in diets for people that want to reduce their gluten intake, but not for people suffering from celiac disease as there are still gluten immunogenic peptides produced upon digestion . Processing has a big effect on the physicochemical properties of gluten, and will, hence, affect the digestive stability, and, hence, the antigenic potential of the protein . Rahaman and colleagues  found that shear by itself does not affect protein digestibility, while pH and temperature substantially affect gluten digestibility and the antigenic characteristics of the hydrolysates that are formed. At pH 3, gluten undergoes acidic deamidation that will lead to a better hydrolysis of the proteins, generating smaller peptide fractions with a lower antigenicity [86,87]. When heating proteins, proteins are aggregating, increasing the resistance of the proteins against digestion 
链接里边的bread, croissants, thin-crust pizza, layer cake and giant pretzels都是烘烤食物。
更正：麸质 = 面筋 = 麦胶 = 谷蛋白 ≠ 麦麸
一袋是超市自己牌子的普通面粉，Ingredients 只写了 bleached flour。我的理解是，bleached 不一定就是用来溴酸钾。到底有没有不知道。
另一袋是超市牌子的未漂白面粉，Ingredients 写了加有 enzyme , 什么酶？不知道。
麸质 = 面筋 = 麦胶 = 谷蛋白 ≠ 麦麸
The change in the genetics of wheet since 1960,such as that of high-yielding dwarf strains, could conceivably account for the recent increased incidence of type 1 diabetes. It's appearance coincides with the increase in celiac disease and other diseases.
《wheat belly》William Davis,MD