杜编提出的这个现象很有意思,我记得有网友在此也说过亲身经历。
美国的小麦和欧洲的小麦本身似乎没有很大的区别,那么在生产和加工环节可能是有区别的。杜编给出的链接中有个评论,提到美国烤面包时用溴酸钾,而欧洲不用。其评论原文如下:
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???
查wiki,得知:
其在发酵、醒发及焙烤工艺过程中起到一种氧化剂的作用,使用了溴酸钾后的面粉更白,制作的面包能快速膨胀,更具有弹性和韧性,在焙烤业被认为是最好的面粉改良剂之一。溴酸钾有致癌性,现在已被許多國家(如欧盟)禁用,但在美国仍允许使用。溴酸钾在足够长的烘烤时间和温度下会耗尽,但是如果在面粉中添加的太多就会有残留。
中华人民共和国卫生部于2005年5月30日发布《2005年第9号公告》称,根据溴酸钾危险性评估结果,决定自2005年7月1日起,取消溴酸钾作为面粉处理剂在小麦粉中使用。在此之前按照《食品添加剂使用卫生标准》(GB2760-1996)使用溴酸钾的食品可以在产品保质期内继续销售。
对面筋不耐受的主要机制是面筋中的麦醇溶蛋白被消化分解产生的多肽进入体内引起过敏反应。在烘焙过程中,麦醇溶蛋白与麦麸中的谷蛋白通过二硫键形成胶联产物,而溴酸钾是氧化剂,减少了该反应的发生。虽然机理还不很清楚,我们也许可以这样假设:
在烘焙过程中,容易产生过敏反应原的麦醇溶蛋白与谷蛋白形成胶联产物,这使麦醇溶蛋白被消化分解成过敏原的机会降低。由于溴酸钾的存在,这种胶联反应受到阻碍,从而麦醇溶蛋白被分解成致敏多肽的机会增加,导致食用者产生面筋不耐受反应。
溴酸钾有致癌的可能,除美国外世界上的主要国家(中国,欧盟等)都禁用溴酸钾作为膨发剂。这可能是杜编观察到“许多麦麸(面筋)不耐受的美国人到了欧洲吃小麦制品平安无事”的原因。
纯属臆测,供讨论,非结论。
对于想进一步了解面包中的溴酸钾的朋友,可参考:
Another Reason to Eat Organic – No Potassium Bromate in Your Bread
主要参考文章:
https://pubs.acs.org/doi/10.1021/jf070639n
Impact of redox agents on the extractability of gluten proteins during bread making.
Abstract
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.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6617089/
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 [81]. 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) [82]. 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 [83] 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)) [84]. 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 [81] and targeted processing of the cereals. One of such novel cereals is tritordeum, a hybrid of durum wheat and wild barley [85]. 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 [85]. 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 [86]. Rahaman and colleagues [86] 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 [86]
https://zh.wikipedia.org/wiki/%E6%BA%B4%E9%85%B8%E9%92%BE
溴酸钾[编辑]
溴酸钾 | |
---|---|
IUPAC名 Potassium bromate |
|
别名 | Potassium bromate(V) Bromic acid, potassium salt |
识别 | |
CAS号 | 7758-01-2 |
PubChem | 23673461 |
ChemSpider | 22852 |
SMILES |
|
InChI |
|
InChIKey | OCATYIAKPYKMPG-REWHXWOFAM |
UN编号 | 1484 |
EINECS | 231-829-8 |
ChEBI | 38211 |
RTECS | EF8725000 |
KEGG | C19295 |
性质 | |
化学式 | KBrO3 |
摩尔质量 | 167.00 g/mol g·mol?¹ |
外观 | 白色結晶粉末 |
密度 | 3.27 g/cm3 |
熔点 | 350 °C(623 K) |
沸点 | 370 °C(643 K) |
溶解性(水) | 3.1 g/100 mL (0 °C) 6.91 g/100 mL (20 °C) 13.3 g/100 mL (40 °C) 49.7 g/100 mL (100 °C) |
溶解性 | 微溶於乙醇 不溶於丙酮 |
结构 | |
晶体结构 | 六邊形 |
热力学 | |
ΔfHm |
-342.5 kJ/mol |
危险性 | |
警示术语 | R:R45 R9 R25 |
安全术语 | S:S53 S45 |
欧盟分类 | Carc. Cat. 2 Toxic (T) Oxidant (O) |
NFPA 704 | |
闪点 | Non-flammable |
致死量或浓度: | |
LD50(中位剂量)
|
157 mg/kg (oral, rat)[1] |
若非注明,所有数据均出自一般条件(25 ℃,100 kPa)下。 |
其在发酵、醒发及焙烤工艺过程中起到一种氧化剂的作用,使用了溴酸钾后的面粉更白,制作的面包能快速膨胀,更具有弹性和韧性,在焙烤业被认为是最好的面粉改良剂之一。溴酸钾有致癌性,现在已被許多國家(如欧盟)禁用,但在美国仍允许使用。溴酸钾在足够长的烘烤时间和温度下会耗尽,但是如果在面粉中添加的太多就会有残留。
中华人民共和国卫生部于2005年5月30日发布《2005年第9号公告》称,根据溴酸钾危险性评估结果,决定自2005年7月1日起,取消溴酸钾作为面粉处理剂在小麦粉中使用。在此之前按照《食品添加剂使用卫生标准》(GB2760-1996)使用溴酸钾的食品可以在产品保质期内继续销售。