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Surdough fermentation (II part)

by luciano

Surdough and phytates
“Increasing fiber content in flour may result in a lower assimilation of minerals complexed by phytates. An optimisation of the fermentation step with surdough allowed to improve both the bioavailability of minerals as well as the sensory attributes of the resulted bread. (16mo. IFOAM Organic World Congress, Modena, Italy, June 16-20, 2008 Archived at ttp://orgprints.org/view/projects/conference.html)”.

Note: Phytic acid is traditionally considered an anti-nutritional factor, ie a substance that can limit the absorption or use of nutrients. In the specific case, by binding to them to form insoluble salts (phytates and phytin), phytic acid hinders the absorption of some minerals (calcium, iron, magnesium and zinc).

Sourdough fermentation and basic baking properties
“Unfortunately, there is often a trade- off between degradation of reactive gluten and retention of gluten for basic baking properties. Large amounts of time and heat may be needed for microbial enzymes to break down problematic pep- tides. To fully degrade the 33-mer α-gliadin peptide in wheat required 24 h at 30 °C (Gallo and others 2005), while durum required 72 h of fermentation at 37 °C to meet gluten-free la- beling standards (De Angelis and others, 2010). HMW glutenins, which are important for baking and pasta integrity, are degraded prior to and more extensively than reactive prolamins during sour- dough fermentation (Ga ̈nzle and others 2008; Wieser and others 2008). Extensively fermented dough has a high ratio of gliadins to glutenins, which is very undesirable for bakers. The disulfide bonds holding together the gluten macropolymer (GMP), an in- tegral component of baking quality, begin to degrade long before glutens. Only 5 h of fermentation with Lactobacilli or acidic chem- icals degraded GMP by up to 46% (Wieser and others 2008). Pentosans, an important component for baking rye bread, were also hydrolyzed in germinated sourdough (Loponen and others 2009). Consequently, the long and hot sourdough fermentation to hydrolyze prolamins compromises functional baking properties of the dough. (A Grounded Guide to Gluten: How Modern Genotypes and Processing Impact Wheat Sensitivity – Chapter Fermentation and microbial enzymes – Lisa Kissing Kucek, Lynn D. Veenstra, Plaimein Amnuaycheewa, and Mark E. Sorrells. Comprehensive Reviews in Food Science and Food Safety Vol. 14, 2015.)”.

Microbiology of sourdough
“It is well known that the type of bacterial flora developed in each fermented food depends on water activity, pH (acidity), minerals concentration, gas concentration, incubation temperature and composition of food matrix (Font de Valdez et. al. 2010). The microflora of raw cereals is composed of bacteria, yeast and fungi (104 – 107 CFU/g), while flour usually contains 2 x 104 – 6 x 106 CFU/g (Stolz, 1999). In sourdough fermentation major role play heterofermentative species of LAB (Salovaara, 1998; Corsetti & Settani, 2007), especially when sourdoughs are prepared in a traditional manner (Corsetti et. al., 2003). Lactobacillus sanfranciscensis, Lactobacillus brevis and Lactobacillus plantarum are the most frequently lactobacilli isolated from sourdough (Gobbetti, 1998; Corsetti et. al. 2001; Valmorri et. al., 2006; Corsetti & Settanni, 2007). The following yeasts have been detected in cereals (9 x 104 CFU/g) and flour (2 x 103 CFU/g): Candida, Cryptococcus, Pichia, Rodothorula, Torulaspora, Trychoporon, Saccharomyces and Sporobolomyces. Saccharomyces cerevisiae is not found in the raw materials. Its occurance in sourdough has been explained by the application of baker’s yeast in most daily bakery practice (Corsetti et. al., 2001). The importance of antagonistic and synergistic interactions between lactobacilli and yeasts are based on the metabolism of carbon hydrates and amino acids and the production of carbon dioxide (Gobetti & Corsetti 1997). Lactic and acetic acid are predominant products of sourdough fermentation). Influence of Acidification on Dough Rheological Properties Daliborka Koceva Komlenić, Vedran Slačanac and Marko Jukić Faculty of Food Technology, Josip Juraj Strossmayer University of Osijek, Croatia 2012- www.intchopen)”.

 

Gluten and intestine

by luciano

Digestion of Gluten Peptides in the Large Intestine

It has been shown that removing gluten from the diet affects the composition of the bacterial community in the large bowel, where the undigested food in the small intestine and could be hydrolyzed by microbial metabolism, generating beneficial compounds for the host.

“Alimentary protein digestion followed by amino acid and peptide absorption in the small intestinal epithelium is considered an efficient process. Nevertheless, unabsorbed dietary proteins enter the human large intestine as a complex mixture of protein and peptides.53,63 The incomplete assimilation of some dietary proteins in the small intestine has been previously demonstrated, even with proteins that are known to be easily digested (e.g., egg protein).64,65 The high proline content of wheat gluten and related proteins renders these proteins resistant to complete digestion in the small intestine. As a result, many high molecular weight gluten oligopeptides arrive in the lower gastrointestinal tract.66 While gluten peptides pass through the large intestine, proteolytic bacteria could participate in the hydrolysis of these peptides. A recent study from our group has shown that some of the gluten ingested in the diet is not completely digested while passing through the gastrointestinal tract, and is consequently eliminated in feces.

Moreover, it has been shown that the amount of gluten peptides present in feces is proportional to the amount of gluten consumed in the diet. Therefore, several gluten peptides are resistant to both human and bacterial proteases in the gastrointestinal tract.66,67

The large intestine is the natural habitat for a large and dynamic bacterial community. Although the small intestine contains a significant density of living bacteria, the density in the large intestine is much higher. The large intestine has as many as 1011–1012 cells per gram of luminal content that belong to thousands of bacterial taxa. Furthermore, the large intestinal microbiota is extremely complex and performs specific tasks that are beneficial to the host.68–71 Among the important functions that the intestinal microbiota performs for the host are several metabolic functions.72 In contrast to the rapid passage of dietetic components through the small intestine, the transit of the luminal material through the large intestine is considerably slower. The longer transit time in the large intestine has been associated with important bacterial metabolic activity.53 Therefore, undigested food in the upper gut could be hydrolyzed by microbial metabolism in the large intestine, generating beneficial compounds for the host.

The resistance of gluten peptides to pancreatic and brush border enzymes allows large amounts of high molecular weight peptides to enter the lower gastrointestinal tract. Therefore, gluten peptides are available for microbial metabolism in the large intestine and could be important to the composition of the intestinal microbiota. It has been shown that removing gluten from the diet affects the composition of the bacterial community in the large bowel.78,79 De Palma et al.78 observed that healthy subjects who followed a gluten-free diet for 1 month had reduced fecal populations of Lactobacillus and Bifidobacterium, but the population of Enterobacteriae such as E. coli appeared to increase. Similar results were obtained in studies with CD patients. Treated CD patients also showed a reduction in the diversity of Lactobacillus and Bifidobacterium species.80,81Gluten Metabolism in Humans. Alberto Caminero, … Javier Casqueiro, in Wheat and Rice in Disease Prevention and Health, 2014”

 

An opportunity to be seized: digestible and tolerable gluten. Why?

by luciano

An opportunity to be seized: digestible and tolerable gluten. Why?

Gluten (it is a protein compound that is formed when glutenin and gliadin, present in flour, are strongly mixed with water) is responsible for celiac disease in genetically predisposed subjects. Not all gluten is at the origin of this pathology: the research has, in fact, isolated some sequences of amino acids (they are the “bricks” that constitute gluten) that are responsible for the adverse reaction of the innate and adaptive human immune system. These sequences are present (even several times) in the molecular chains (peptides) that constitute gluten, and, above all in gliadins. There are many studies that aim to create grains or flours without these sequences, mixtures where the action of particular bacteria present in the acid paste destroy the toxic fractions. Particular enzymes (proteases produced by Aspergillus) have been identified that can activate a complete enzymatic digestion of gliadin, reducing or eliminating the reactive response of gluten-sensitive T cells. (Toft-Hansen H et al Clin Immunol. 2014 Aug; 153 (2): 323-31. Doi: 10.1016 / j.clim.2014.05.009. Epub 2014 Jun 3).

Gluten is indigestible as such, only if divided into constituent amino acids it can be digested and, after being passed into the blood, be assimilated. The action of “chopping up the gluten is carried out by the enzyme pepsin (it is the most important of the digestive enzymes and, activated by hydrochloric acid, attacks proteins and breaks them down into fragments called polypeptides which will then be broken down into individual amino acids by trypsin ), present in the stomach and the enzyme trypsin produced by the pancreas present in the intestine. These two enzymes are not always able to “break up” the gluten and the residues are eliminated by “normal” people. These residues, on the other hand, if they contain toxic sequences activate the response of the immune system that fights them as “enemies”. The more gluten is strong (ie the stronger the bonds of the molecules that make up gluten) the more difficult and the action of enzymes will be longer. You can be born celiac but you can also become genetically predisposed. At greater risk, of course, are the relatives and relatives of celiacs. Scientific research has shown that the use in the diet of foods produced with grains as light as possible and tolerable (with the least possible amount of “toxic epitopes”) reduces the possibility of becoming celiac and is indicated for non-celiac gluten sensitive people. An example regarding the monococcus wheat we find in the study:

“…..Conclusions: Our study shows that Tm (Grano Monococco) is toxic for CD patients as judged on histological and serological criteria, but it was well tolerated by the majority of patients, suggesting that Tm is not a safe cereal for celiacs, but that it may be of value for patients with gluten sensitivity or for prevention of CD.Copyright of European Journal of Nutrition is the property of Springer Science & Business Media B.V. and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder’s express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.”

For some time now, scientific research has highlighted another gluten-related disease: non-celiac gluten sensitivity (NCGS). Today it is possible to diagnose it only through a long and complex series of analyzes which, for this reason, cannot be widely applied. The research (well summarized in the attached research) is still on the high seas, in fact, in the realization of biomarkers suitable to diagnose this pathology in a certain and simple way. Finally it should be noted that although there are very many studies, researches and tests on patients, these have proved too partial to be able to define “with certainty” how the NCGS is activated. Gliadins, however, play an important role as anti-gliadin antigen has been found in patients diagnosed with this disease. Finally, the research showed that a light and tolerable gluten is less invasive for those with irritable bowel disease.