Nutriment with low amounts of allergens

Abstract

There is provided a method for treatment of oat, said method comprising the sequential steps of a) providing oat kernels, b) heat treating the oat kernels in a temperature in the interval 95 - 100°C, c) processing the oat kernels in a disc mill with discs, to obtain milled oat kernels and d) subjecting the milled oat kernels to a separation with respect to size to obtain at least one finer product fraction and at least one coarser fraction. Technical effects include that it is possible to provide an oat flour, which is reduced in prolamins in particular compounds causing dietary sensitivities and disorders in patients diagnosed with Celiac Disease. The method is suitable for large scale manufacture, not the least since the separation is carried out in a dry state. All of the oat kernels can be recovered and used for different purposes so that no part of the oat kernels have to be discarded.

Description

[0001]Nutriment with low amounts of allergens Field of invention The present invention relates to a method of preparing and separating different parts from oat kernels in order to minimize the amount of certain proteins / peptides that may cause dietary sensitivities and disorders. There is further provided some flour, made with a method as well as a nutriment such as bread, made with an ingredient manufactured according to the method. Background A gluten-free diet is currently the only effective means of treating individuals with Celiac disease (CD). Such a diet enables celiac patients to control their symptoms and avoid complications associated with this condition. However, though the quality of gluten-free foods has been improved during recent years, maintenance of a gluten-free diet does not necessarily ensure an adequate nutritional intake. Because oats are an important source of proteins, lipids, vitamins, minerals, and fibre, their inclusion in a gluten-free diet might improve the nutritional status of a celiac patient. Although oats are included on the list of gluten-free ingredients, approved by European regulations, their safety when consumed by celiac patients remains debatable. Some studies claim that pure oats are safe for most celiac people, though contamination with other cereals like wheat might be the main problem facing people with Celiac disease. However, it is necessary to consider that oats include many varieties, containing various amino acid sequences showing different immunoreactivities associated with the toxic prolamins. As a result, several studies have shown that the immunogenicity of oats varies depending on the cultivar consumed. Thus, it is essential to thoroughly study the variety of oats used in a food ingredient before including it in a gluten-free diet. Ref. Isabel Comino et al. 2015 Nov 7; 21(41): 11825–11831. A therapeutic gluten-free diet often has nutritional limitations. Nutritional qualities such as protein content, presence of biologically active and beneficial substances (fibre, beta-glucans, polyunsaturated fatty acids, essential amino acids, antioxidants, vitamins, and minerals), and tolerance by the majority of celiac patients make oat popular for use in gluten-free diet. The health risk of long-time consumption of oat by celiac patients is a matter of debate. The introduction of oat into the diet is only recommended for celiac patients in remission. Furthermore, not every variety of oat is appropriate in a gluten-free diet. The risk of sensitization and an adverse immunologically mediated reaction is a real threat to some celiac patients. Several unsolved issues still exist which include the following: (1) determination of the susceptibility markers for the subgroup of celiac patients who are at risk because they do not tolerate dietary oat, (2) identification of suitable varieties of oat and estimating the safe dose of oat for the diet, and (3) optimization of methods for detecting the gliadin contamination in raw oat used in gluten-free diets. Ref. Iva Hoffman et al. Nutrients, 2019 Oct; 11(10): 2345. Gluten is important to retain gas to obtain the desired volume and texture in a dough system. It is essential to form a strong protein network required for the desired viscoelasticity. Prolamin and glutenin are the major fractions of the gluten. While prolamin and glutenin provides viscosity and extensibility in a dough system, glutenin is responsible for the elastic and cohesive properties of dough. Gluten is important not only for appearance, but also for crumb structure of cereal-based products. Ilkem Demirkesen et al.Journal of Food Engineering Vol.96 Jan. 2010, Pages 295-303. Prolamins are a group of plant storage proteins that are primarily found in cereal grains. They are a subgroup of proteins known as seed storage proteins, which serve as a source of nutrients for the developing plant embryo. Prolamins are characterized by their high content of the amino acid residues proline and glutamine. Different types of cereals contain different prolamins. For instance, oat comprises avenin. These prolamins contribute to the unique properties of each cereal grain, such as the elasticity of wheat dough or the thickening properties of cornstarch. Prolamins including avenin and globulin, historically also gluten, have received attention due to their role in certain dietary sensitivities and disorders. Oat is by nature gluten free, but sometimes oat is grown adjacent to wheat, barley and rye, and then risk becoming contaminated by these other grains. It may rise the problems for sensitive individuals including people with Celiac disease, irritable bowel syndrome (IBS) or similar gut disorders. Some individuals may react to their lectin content, although low compared to effect from gluten in wheat, barley, and rye, see Leišová-Svobodová, et al in Sci Rep 12, 8660 (2022). The major storage protein fractions in cereal grains are defined as prolamins based on their solubility in mixtures of alcohol and water and their high contents of glutamine and proline. These proteins account for up to 80 wt% in wheat, barley and rye, but to a less extent in oats. Proteins from wheat (gluten) form a visco-elastic network when mixed with water, which enables production of leavened bread and other bakery products. As these properties are not shared by the prolamins in barley or rye, wheat therefore has gained in importance among bakers. The prolamins from different cereal species are termed as gliadins (wheat), hordeins (barley or secalins (rye). A further group, found in oats are called Avenins. The safety of oats for people with Celiac disease caused by allergens like gluten is unresolved. While oats have attractive nutritional properties, which can improve the quality and palatability rigorous feeding studies to address the safety of oat is called upon. A Number of key avenin peptides that stimulate the pathogenic gluten- specific T cells in CD patients in vivo has been defined. One of these peptides is Avena Sativa, an allergen that belongs to the gliadin / glutenin family. Avenins are one of the most serious causes of Celiac disease, also known as celiac sprue or gluten sensitive enteropathy. Q09114 is a known allergen in oat and since it is well characterized it is chosen to represent allergens in oat. Q09114 comprises 182 amino acid residues. Q09114 is well studied because it is a notorious allergen in oat and causes problems for many sensitive individuals. Isolation of oat prolamin proteins (Avenins), i.e. allergens or analysis of a possible gluten contamination or other allergens, which will cause non-specific effects and symptoms is essential, and therefore the basis for this analysis. Ref. Greg. Tanner et al. Front. Nutr. 2019 Oct 15:6:162, Rocher et al, FEBS Lett 310, (1)37-40 (1992); Michelle Lisa Colgrave et al. Frontiers in Nutrition 2021 May 06 vol B Article 680413. WO 2019 / 094585 discloses a process comprising tempering whole grain with a moisture content of 15 to 20 wt%. It is heated to a temperature of about 140 °C to about 160 °C for about 13 to 20 minutes; before conditioning and milling to form a bran and germ component and a bread flour component. WO 2009 / 038938 describes a method to form an oat bran fraction and oat flour fraction. Claim 6, further describes a dry heating step before milling where oat groats are heated up at to about 85 to 110°C for about 70 to 110 minutes to provide steamed and toasted oat groats having a moisture content of about 9 to 14%. WO 2008 / 096044 discloses a method for fractionating oat, where lipid concentrates from oat by extracting non-heat- treated oat with a fluid in a supercritical state. Moltenberg et. al. in Cereal Chem. 73 (5):579-587 describes heating procedures before milling, included soaking oats in water for 2 min, followed by steaming for 10 min at 100°C and drying in paper bags at 100°C. EP 0937411 discloses a process for manufacturing an oat containing cereal product of improved stability. In the claim, an oat material is pre-oxidized by pre-oxidizing dehulled, steamed and kilned oat groats, flakes or flour by using a temperature of from 120 to 135°C for about 2 to 45 min during kilning, to obtain a pre-oxidized comminuted oat material having a pregelatinizing degree of 25 to 50%. This is followed by a heat treatment at 100 to 250 °C for 2 s to 60 min. J.Ray Runyon et al in Journal of Cereal Science, volume 65, September 2015, Pages 119-124 studied the effect of heat treatment on the soluble protein content in oat groats. The total amount of soluble protein (with respect to total protein) was reduced in heat treated oats. The ratio of monomeric to globulin hexamer and aggregate proteins was reduced because of heat treatment. There is disclosed a selective elimination of protein bands associated with the albumin and prolamin protein fractions because of heat treatment. The globulin proteins were found to be less sensitive to heat treatment. The heat treatment of oats was steaming at 102 °C for 50 minutes followed by drying at 110-120 °C for 50 minutes. Summary One object of the present invention is to obviate at least some of the disadvantages in the prior art and to provide a new dry method of extracting prolamins actually certain Avenins from oat. Avenins that cause an allergic reaction especially in man diagnosed with Celiac disease. In a first aspect there is provided a method for treatment of oat, said method comprising the sequential steps of: a. providing oat kernels, b. heat treating the oat kernels in a temperature in the interval 95 - 100 °C, c. processing the oat kernels in a disc mill to obtain conjugates from crumbled oat kernels and fractions from conjugates. d. subjecting the milled oat kernels to a separation with respect to size to obtain at least one finer product fraction and at least one coarser fraction. In a second aspect there is provided an oat flour wherein the amount of each of the proteins with accession numbers Q09114, L0L4J1, L0L6J0, L0L5H3, Q2EPY2, L0L5I0, I4EP88, L0L5H5, L0L5G8, L0L6K1, Q09072, Q09071, L0L6J7, L0L837, L0L8A4, and L0L8A0 from Avena Sativa are reduced with at least 50 wt%. In a third aspect there is provided a nutriment, which nutrient is made with at least one ingredient, which ingredient is made according to the method as described above. An advantage is that a flour, having a very low amount of prolamin lectins such as Avenin, is provided. The method is suitable for large scale manufacturing, not the least since the separation is carried out in dry state. After the separation both the finer fraction and the coarser fraction can be utilized for various purposes, which implies that no part of the oat kernels has to be wasted. Yet another advantage is that by eliminating important parts of the prolamins and glutenin, it is possible to make a bread with a high amount of oat, which bread becomes more porous compared to bread baked with oat according to the state of the art. Thus, normal porous bread can be baked with oat-flour according to the invention. Further embodiments of the present invention are defined in the appended dependent claims. Brief description of the drawings Aspects and embodiments will be described with reference to the following drawings in which: Figure 1 shows a schematic representation of one embodiment of the method according to the invention with the steps a) providing oat, b) peeling the oat to provide oat kernels, c) heat treating the oat kernels in a temperature in the interval 95 – 100 °C, d) disc milling, and e) size separation. Figure 2 shows two breads cut in the middle. Both are based on the same raw-materials and identical recipe containing much more than 50 wt% oat. Bread A is based on peeled oat kernels. Bread B is based on the fine fractioned depleted prolamin meal according to the present invention. Both have passed a sift with an aperture of 0.300 µm. For a chemical analysis of bread A and B see table 1 and 2. Ref. E.Hϋttner et al.J, of Cereal Science, Vol 52 July 2010, pages 65-71. Figure 3 shows results from example 3 with a PCA plot that shows clusters of samples based on similarities in their proteome. PC1 reveals the most variation, while PC2 reveals the second most variation. Figure 4 shows a volcano plot from example 3. The points above the curve denote significantly changed proteins. Set filters p value 0.05 and FDR 0.05 after permutation based multiple testing. Downregulated in depleted sample = higher amount in Zero sample. Dots below the curve indicate peptides not detected in depleted samples. Only detected in zero samples, or not significant. Detailed description Before the invention is disclosed and described in detail, it is to be understood that this invention is not limited to particular configurations, process steps and materials disclosed herein as such configurations, process steps and materials may vary mostly because of seasonal and / or biological reasons. It must be noted that, as used in this specification and the appended claims, the singular forms “a”, “an” and “the” include plural referents unless the context clearly dictates otherwise. In the first aspect there is provided a method for treatment of oat, said method comprising the sequential steps of: a. providing oat kernels, b. heat treating the oat kernels in a temperature in the interval 95 - 100 °C, c. processing the oat kernels in a disc mill with discs, to obtain milled oat kernels, d. subjecting the milled oat kernels to a separation with respect to size to obtain at least one finer product fraction and at least one coarser fraction. Peeling of oat is carried out by known standard methods. In one embodiment, the oat kernels are purchased. In another embodiment, the oat kernels are made from oat by peeling the oat to obtain oat kernels. The method can be carried out both batch-wise as well as in a continuous mode. In one embodiment, certain quality standards are applied for the oat kernels provided in step a). In another embodiment, the volume weight should be at least 700 grams per litre of oat kernels. In one embodiment, the amount of gluten in oat kernels meant for gluten-free food shall be less than 20 ppm. In one embodiment, the amount of water should be less than 14 wt%. After the heat treatment, the oat kernels are dried with hot air, but not warmer than 70 °C. Table 1 Provided unprocessed Oat kernels. Chemical composition. Fat SBRII 6.9 wt% Starch 57.7 wt% Protein 9.9 wt% B-glucan n.d. wt% Dietary fiber 6.1 wt% Water holding Capacity (WHC)* 1.5 g - 2.1 g water / g fraction. * The water holding capacity (WHC) was measured as outlined in LWT Vol 16315 June 2022. I.Jokinen et al. Water holding capacity (WHC) is a significant factor informing of the hydrothermal efficacy, applied on the e.g. starch and protein containing kernels measured after drying. Regarding the Water Holding Capacity (WHC) in the finer fraction, it is in one embodiment 0.65 g water absorbed per 1 g dry flour (Range 0.54-0.75). In general the water holding capacity of the at least one finer product fraction according to the present invention, is lower compared to many other similar products. The reason is due to the heat treatment and subsequent separation. This treatment removes certain components inter alia allergens and also components of oat which are responsible for the water holding capacity. The oat kernels are in one embodiment heat treated at about 100 °C. In one embodiment, the heat treatment is carried out with steam. The oat kernels are heat treated at a temperature in the range 95 - 100 °C. In one embodiment the heat treatment is carried out under stirring. The heat treated oat kernels are processed in a disc mill between discs, which rotate in relation to each other. Either of or both of the discs can rotate. It is important that the distance between the discs is adjusted according to the size of the oat kernels, which in one embodiment is about 0.7 mm. The distance depends on the oat kernels and can thus vary. The distance between the discs is important to control when deciding how much of the outer parts shall be removed from the oat kernels. The gradual removal of material from the outside of the oat kernels during disc milling, makes it possible to separate as much of the oat surface material as desired. This meet the requirements when separation of certain proteins / peptides are depleted from the rest of the kernel. It has turned out that the historical problems regarding oat milling have much to do with the fat content, as the fat easily gives sticky properties and severely hampers the customary dry milling and sifting during the previous years. After extensive research, the inventor has found that the separation and milling problems, well-known to everyone within the field, now can be solved by preparing oat and other grains by the present innovation. Without wishing to be bound by any particular scientific theory, the inventor by experience and tests, argues that a careful heat treatment in combination with the next step – disc milling - contributes to a change in the oat kernels organising the fat, starch and protein in the oat into conjugates. These conjugates can thereafter be separated in a dry state using the special subsequent disc milling process. In the disc mill, the material is fed via the mill centre and the milled fractions is collected outside the periphery of the discs. In one embodiment, the discs spin at a high-speed relative to each other. In one embodiment, the discs spin at a speed in the interval 2000 – 6000 rpm relative to each other. Table 2 The fine fraction which passed the 630 µm sift has the following chemical content as measured in one example. Fat SBRII 6 wt% Starch 63 wt% Protein 9 wt% B-glucan 2 wt% Dietary fiber 4 wt% Water holding Capacity (WHC) 0.54–0.75g water / g fraction. After the disc milling process, the milled oat fractions are separated from each other with respect to size and level of allergens, where the finer fraction (65%) having a low level of allergens, whereas the coarser fraction (35%) having a higher level of allergens, β-glucan, protein and other valuable nutrients. This applies to at least some known allergens in oat. An advantage is that the milling process can be carried out on dry kernels allowing a subsequent separation within a sieve in dry state. The fine fraction is a safe food for people suffering from Celiac disease. The coarser fraction is valuable because of its high content of β-glucan and protein. Both can be used for food where the prolamin content including avenin is not critical. Alternatively, the β-glucan can be extracted in a further step, which may also be a dry step. A qualified report presenting materials, methods and results is visualized below, where “N” represents four separate samples functioning as a control group and “D” represents the four samples handled in accordance with the present invention. In one embodiment, the amount of at least some proteins and / or peptides known to cause dietary sensitivities and disorders in some individuals in the at least one finer product fraction is reduced compared to the oat kernels provided in step a). In one embodiment, the amount of at least some allergens in the at least one finer product fraction is reduced compared to the oat kernels provided in step a). Such proteins / peptides and allergens may vary, but in one embodiment the protein denoted Q09114 is taken as a representative protein form this group. In one embodiment, the level of prolamin in the at least one finer product fraction is significantly reduced compared to the oat kernels provided in step a). The oat kernels in step a) constitute a control group i.e. a group “N” and being the control group in the report presented below. In particular the proteins and / or peptides causing dietary sensitivities and disorders in some individuals are reduced to a level where the product is tolerable to most individuals. In one embodiment, the heat treating in step b) is hydrothermal. The heat treating in step b) is performed at a temperature in the interval 95 – 100 °C. In one embodiment, the heat treating in step b) is performed for 20-60 minutes. The heat treatment should be performed at atmospheric pressure. In one embodiment, the heat treating in step b) is carried out with steam at atmospheric pressure. Depending on the exact air pressure, the steam temperature can vary slightly up to 100 °C. The heat treatment is in one embodiment conducted under stirring so the oat kernels prevent from lumping together. The stirring will also secure a thorough and even temperature rise. Lumping together suggests a high humidity, wrongly implying a more serious partial gelatinization among certain kernel groups. A slow Rotation of the process vessel stirrers can be used for the mixing during the heat treatment. In one embodiment, the heat treating in step b) is carried out in a process vessel at atmospheric pressure by supplying steam until the temperature throughout the entire process vessel has reached 95-100 °C, whereby the treatment is continued for a period of time in the interval 20-60 minutes. In one embodiment, a drying step is performed between steps b) and c), in which the drying step comprises supply of heated air to the treated oat kernels from step b). If steam has been used for the heat treatment, heated air is preferred because of unexpected high humidity in the kernels. Dry kernels facilitate the subsequent dry separation during milling and sifting. In another embodiment, the drying step is carried out until the water content in the treated oat kernels is below 15 wt%, preferably below 14 wt%, more preferably below 13 wt%, most preferably below 12 wt%. In one embodiment, the drying step is performed by supplying air with a temperature in the interval 50 – 60 °C. A temperature above 70 °C should be avoided in the drying step. Thereby minimizing the risk of an unfavourable starch modification maybe hampering a future dough making process. During the disc milling the process shall be supervised so that the oat fractions meet the demand of desired properties. The distance between the discs is very important and be adapted to the oat kernel size. In one embodiment, the oat kernels shall be separated with respect to their volume weight before step a) begins. In case of a volume weight < than 700 g / litre, a control sieving might be a good strategy, especially if the oat kernel batch turns up with a volume weight << than 700 g / L. It would also be possible to use oat kernels with a size in the interval 2.0 – 2.2 mm. For such oat kernels a suitable distance between the discs is about 1.05 mm. It is also possible to use larger oat kernels. If yet larger oat kernels will be used the distance between the discs should be adjusted accordingly. In one embodiment, the disc mill in step c) has a distance between the discs in the range 0.60 to 1.20 mm. In one embodiment the disc mill in step c) has a distance between the discs in the range 0.75 to 1.20 mm. In one embodiment the disc mill in step c) has a distance between the discs in the range 0.70 to 1.10 mm. In one embodiment the disc mill in step c) had a distance between the discs of 1.05 to 1.15 mm, preferably 0.90 to 1.10 mm, more preferably 0.95 to 1.05. In an alternative embodiment the disc mill in step c) has a distance between the discs in the interval 0.6 to 0.8 mm, preferably 0.68 to 0.75, more preferably 0.68 to 0.72. All interval changes are in one embodiment made by hand, assisted by a stationary micrometre installation, frequently checked by a steel feeler gauge. The discs should be adapted to the size of the oat kernels, so that a small distance is used for smaller oat kernels and a larger distance for larger oat kernels. In order to have a favourable distribution of the different fractions, the disc milling shall be supervised so that the processing of oat kernels follows present directives. In one embodiment, the rotation direction of the disc mill in step c) can be alternated. The discs rotate relative to each other. For instance, one disc can rotate, and one disc can be stationary. Alternatively, both discs can rotate. One disc or both discs can have a varied groove pattern allowing further possibilities to fine tune the process. The grooves provide further possibilities of fine-tuning the milling. In one embodiment, standard corrugated discs are used. In connection with a grooved pattern, it is also possible to change the direction of rotation, in particular for discs with groves. This provides additional possibilities to fine tune properties of the disc mill. In one embodiment, the size separation in step d) is carried out by sifting. Sifting is suitable for separation in large scale. In one embodiment, the separation in step d) is performed with a sift with a nominal aperture size in the interval 430 – 830 µm according to ASTM E11. In one embodiment, the separation in step d) is performed in more than one step with at least two different sifts. In one embodiment, the separation in step d) is first performed with a first sift with a nominal aperture size in the interval 430 – 800 µm according to ASTM E11 and subsequently a second sift with a nominal aperture size in the interval 801 – 1200 µm according to ASTM E11. In one embodiment, the at least one finer product fraction is recovered and used in food or feed. The at least one finer product fraction is also denoted as an oat flour. This fine fraction is suitable for food where a low level of allergens is desired. Also, certain animals may be sensitive for prolamins including avenin so the fine fraction can also be used for animal feed. In one embodiment, the at least one coarser fraction is recovered and used in food or feed. This fraction can be used when the content of prolamin including avenin is not critical and when a high content of β-glucan is desired. In one embodiment, the at least one coarser fraction is recovered and subjected to at least one further separation step to enrich at least β-glucan. β-glucan is a valuable nutrient and can for instance be a food additive. For persons which are not sensitive to certain components in oat, also the at least one coarser fraction is suitable to eat. The higher amount of allergens in the at least one coarser fraction is not a problem for individuals which are not sensitive or allergic and the at least one coarser fraction comprises many compounds which are useful for food. In the second aspect there is provided an oat flour wherein the amount of each of the proteins with accession numbers Q09114, L0L4J1, L0L6J0, L0L5H3, Q2EPY2, L0L5I0, I4EP88, L0L5H5, L0L5G8, L0L6K1, Q09072, Q09071, L0L6J7, L0L837, L0L8A4, and L0L8A0 from Avena Sativa are reduced with at least 50 wt%. The proteins are denoted by their accession numbers and further information about the proteins can be retrieved for instance from the website https: / / www.ncbi.nlm.nih.gov / All of the mentioned proteins are reduced by at least 50 wt% compared to the oat before a reducing treatment. The different proteins can be reduced to different extents although always exceeding 50 wt%. The proteins Q09114, L0L4J1, L0L6J0, L0L5H3, Q2EPY2, L0L5I0, I4EP88, L0L5H5, L0L5G8, L0L6K1, Q09072, Q09071, L0L6J7, L0L837, L0L8A4, and L0L8A0 are present in oat, Avena Sativa and are known to cause problems to sensitive individuals. All those proteins are reduced with at least 50 wt% according to the present invention, i.e. at least 50 wt% of the amount of each protein is removed according to the invention. In an alternative embodiment, at least 65 wt% of the amount of each protein is removed according to the invention. In an alternative embodiment, at least 75 wt% of the amount of each protein is removed according to the invention. In an alternative embodiment, at least 85 wt% of the amount of each protein is removed according to the invention. It is shown in the experimental section that the remaining amount of these proteins varies between 2 – 11 wt%, i.e. 89 – 98 wt% of the proteins is removed. The reduction of the proteins is measured as described in the experimental section. In one embodiment, the oat flour has a water holding capacity (WHC) of less than 0.6 ml / g product as measured according to LWT Vol 16315 June 2022. I.Jokinen et al. This measurement method is used throughout to measure the water holding capacity (WHC). In one embodiment the amount of the protein with accession code Q09114, has been reduced with at least 90 wt%, preferably at least 95 wt%, more preferably at least 98 wt%, compared to the original oat. The protein with accession code Q09114 is a notorious and well known allergen, causing problems for sensitive individuals. In one embodiment, the oat flour is at least one finer product fraction manufactured according to the above mentioned method. In the second aspect there is provided an oat flour manufactured with the method described above. This flour can be used for food also for sensitive individuals, at least for most individuals of this kind. In the third aspect there is provided a nutriment, which nutrient is made with at least one ingredient, which ingredient comprises an oat flour as described above. In one embodiment, the nutriment is a food and wherein at least 52 wt% of all ingredients are the at least one finer product fraction according to the method as described above. In one embodiment at least 55 wt% of all ingredients are the at least one finer product fraction. In one embodiment at least 60 wt% of all ingredients are the at least one finer product fraction. In one embodiment at least 70 wt% of all ingredients are the at least one finer product fraction. In one embodiment at least 80 wt% of all ingredients are the at least one finer product fraction. In one embodiment the nutriment is bread. The use of the finer fraction from the method makes it possible to bake a bread with normal porosity. If the bread would be baked with an oat flour which has not been processed according to the present invention, then the bread would become much more compact and would not have the desired porosity.   Bread porosity refers to the volume fraction of air pockets within the bread's crumb structure. It is a measure of the bread's texture, indicating the lightness and openness of the crumb, which results from the fermentation and baking processes. Bread porosity is thus the ratio of the volume of the air pockets (pores) within the bread to the total volume of the bread. Normal bread has a porosity of about 40 – 60 %. In one embodiment the bread has a porosity of at least 40%. In one embodiment the bread has a porosity of at least 50%. In one embodiment the bread has a porosity of at least 55%. In the third aspect there is provided a nutriment, which nutrient is made with at least one ingredient, which ingredient is made according to the method as described above. Examples of Nutriments include but are not limited to bread and pancakes. Such a Nutriment has a high nutritional value and be tolerated by sensitive individuals. In one embodiment, a dough for bread is made using the at least one ingredient and wherein the dough is baked to obtain a nutriment with excellent porosity larger than 52%. Other features of the invention and their associated advantages will be evident to a person skilled in the art upon reading the description and the examples. It is understood that the disclosed embodiments can be freely combined with all other embodiments as long as it is not clearly contradictory. It is to be understood that this invention is not limited to the particular embodiments shown here. The following examples are provided for illustrative purposes. In the following, each of the described methods, apparatuses, examples and aspects, which do not fully correspond to the invention as defined in the claims is thus not according to the invention and is, as well as the whole following description, present for illustration purposes only or to highlight specific aspects or features of the claims. Examples Example 1 Oat kernels were purchased. The oat kernels were analyzed, and it was ensured that the oat kernels met the following specifications: ^ Minimum volume weight per liter: 700 grams ^ Gluten: less than 20 wt. ppm (to ensure that the oat is not contaminated by other crops.) ^ Maximum water content: 14 wt%. Measured according to Official AOAC Methods of Analysis Two batches of oat kernels with a weight of 2000 kg and 500 kg respectively were filled in a process vessel and steam was supplied to the vessel. When the temperature inside the entire vessel had reached 99 °C, then the steam was supplied in additionally 37 minutes. There after the steam supply was cut off and the treated oat kernels were supplied with heated air at a temperature in the interval 50-60 °C to dry the kernels. The oat kernels were slowly stirred both during the steam treatment and during the drying. The oat kernels were dried until the water content was 13 wt%. The treated and dried oat kernels were milled in a disc mill Engsko MHA600. The discs were grooved with grooves extending in a direction from the inner part of the disc to the outer part. The distance between the discs was adjusted to 0.70 mm. The distance was measured with a steel feeler gauge. Thus, the distance between the discs was measured from the outermost part of grooved discs so that the shortest distance between the discs is measured. After the milling the material was sifted in a sift Engsko FS1000. The sifting was performed in two stages with a first sift with a nominal aperture size of 630 µm according to ASTM E11 and a second sift with a nominal aperture size of 1000 µm according to ASTM E11. This gave one coarser fraction which did not pass any of the sifts and one fine fraction which passed the 630 µm sift and a middle fraction which passed the 1000 µm sift. Example 2 Nutriment meant to use an oat flour liberated from allergens like gluten- and prolamin instead of wheat meal according to this invention. The gluten- and prolamin free Nutriment proposes a tasty, soft and porous loaf, very much alike what is available on Super market. Recipe; 50 g potato flour, 10 g salt, 15 g sugar 6 g psyllium were mixed into a first mixture. 430 grams of finger warm water was mixed with 5 / 20g of dry / fresh yeast, then added to the first mixture. 434 grams of the fine fraction from example 1 was added step by step to obtain a dough. The dough was added to a loaf pan. The dough was allowed to rise at 33 °C for 45 minutes. The dough was baked in an oven at 200 °C, until the inner temperature of the loaf had reached 99 °C. The loaf was placed on a grate and allowed to cool under a cloth. The load was cut in half and inspected (Fig. 2). Example 3 Material and methods Four control oat samples (n=4) and four depleted oat samples (n=4), all coming from the Scandinavian oat Belinda family were produced by Maryhill AB in Helsingborg Sweden. Before the proteomic analysis started, the two groups (eight samples) were individually analysed for total amino acids and Kjeldahl nitrogen by Eurofins / Steins Laboratory. The depleted oat samples were manufactured according to the present invention. Aminoacids and Kjeldahl nitrogen see Table 4. Table 4.Control=N Depleted=D Aminosyror Sample Sample D->N % N D Lys 0.511 0.361 70.646 Thr 0.424 0.319 75.236 Iso 0.421 0.32 76.010 Leu 0.871 0.645 74.053 His 0.264 0.185 70.076 Phe 0.616 0.466 75.649 Tyr 0.457 0.342 74.836 Val 0.626 0.459 73.323 Ala 0.574 0.409 71.254 Arg 0.838 0.596 71.122 Asp 1.02 0.724 70.980 Glu 2.43 1.85 76.132 Gly 0.624 0.441 70.673 Hydroxy P n.a. Orn n.a. Pro 0.626 0.455 72.684 Ser 0.586 0.431 73.549 Cys+Cys 0.378 0.295 78.042 Met 0.224 0.169 75.446 Try 0.172 0.142 82.558 Gram AA:% 11.662 8.609 73.821 Kjeldahl 12.2 9.5 77.9 protein AA:Protein % 95.6 90.5 94.8 Aminoacids i Eurofins / Steins oat samples (Average g / 100g N) Methods Proteins were extracted from samples using lysis buffer [2% sodium dodecyl sulfate (SDS), 50 mM triethylammonium bicarbonate (TEAB)] and the FastPrep®-24 instrument (MP Biomedicals). Protein concentration in the lysates was determined using Pierce™ BCA Protein Assay Kit (Thermo Scientific) with bovine serum albumin (BSA) solutions as standards. Samples (30 µg) were processed using a modified filter-aided sample preparation (FASP) method.17 Briefly, samples were reduced in 100 mM dithiothreitol (DTT) for 30 min at 56 °C, transferred to Microcon-30kDa Centrifugal Filter Units (Merck), washed several times with 8 M urea, and alkylated in 375mM iodoacetamide (IAA) for 30 min at room temperature (RT). Samples were digested at 37 °C overnight with chymotrypsin (Pierce MS grade chymotrypsin; dilution ratio of 1:100; Thermo Fisher Scientific) in digestion buffer (0.5% sodium deoxycholate (SDC), 50 mM TEAB) and an additional portion was added next day and incubated for another 3 hours. Peptides were collected by centrifugation and labelled using TMTpro isobaric mass tagging reagents according to the manufacturer's instructions. The samples were combined into one TMT-set and the SDC was removed by acidification (10% trifluoroacetic acid). The set was desalted (Pierce peptide desalting spin columns; Thermo Fischer Scientific) according to the manufacturer's instructions and pre- fractionated into 20 fractions with basic reversed-phase chromatography (XBridge BEH C18 column, 3.5 μm, 3.0 × 150 mm; Waters) using the Dionex Ultimate 3000 UPLC system (Thermo Fischer Scientific) and a gradient of 3%–90% acetonitrile in 10 mM ammonium formate buffer (pH 10), run over a period of 25 min. Nano-Liquid chromatography mass spectrometry (nLCMS) analysis and database matching replaced conventional LC techniques. Each fraction was analysed on Orbitrap Lumos™ Tribrid™ mass spectrometer equipped with the FAIMS Pro ion mobility system interfaced with nLC 1200 liquid chromatography system (all Thermo Fisher Scientific). Peptides were trapped on an Acclaim Pepmap 100 C18 trap column (100 μm x 2 cm, particle size 5 μm, Thermo Fischer Scientific) and separated on an in-house constructed analytical column (350x0.075 mm I.D.) packed with 3 μm Reprosil-Pur C18-AQ particles (Dr. Maisch, Germany) using a gradient from 3% to 80% acetonitrile in 0.2% formic acid over 90 min at a flow of 300 nL / min. FAIMS Pro was alternating between the compensation voltages (CV) of -50 and -70, and essentially the same data-dependent settings were used at both CVs. Precursor ion mass spectra were acquired at 120 000 resolution and MS2 analysis was performed in a data- dependent mode, where the most intense doubly or multiply charged precursors were isolated in the quadrupole with a 0.7 m / z isolation window and dynamic exclusion within 10 ppm for 45 s. The isolated precursors were fragmented by collision induced dissociation (CID) at 30% collision energy for 3 s (‘top speed’ setting) and detected in the ion trap, followed by MS3 multinotch (simultaneous) isolation of the top 10 MS2 fragment ions by higher-energy collision dissociation (HCD) at 55% collision energy and detection in the Orbitrap at 50000 resolution m / z range 100-500. The MS-data was matched against the oat database Glurp v5.0 (Ref M. Daly et al, Front Nutra. 2020 Jul 17:7:87. Doi: 10.3389). Quantitation with isobaric tandem mass tags (TMT) labeling was used to compare abundance of peptides and their corresponding proteins at a global level in several samples in parallel. In the present study 30µg pure protein samples were extracted from both the protein in the depleted oat and the control oat samples thereafter cleaved into peptides with chymotrypsin. Identical peptides, derived from different samples, were indistinguishable in their intact form during fractionation, separation, and analysis. From the classical literature “The Vegetable Proteins 1909”, published again by The Cornell University Library Collections in 1995, the solubility of vegetable proteins by alcohol were investigated and found to be 70-90 wt%. The solubility was later reported by Tanner G.et al to be 85 wt% and the soluble proteins contained 96 wt% Avenin. Ref. Front. Nutr. 2019, Oct 15:6162. In table 6 you will find the number of peptides found in the control group, M.v. 1.96025 (n=4). The number of peptides found in the depleted group was M.v. 0.03975 (n=4). Calculated as number of depleted peptides (average 0.03975) relative to the number of peptides in the control group (M.v. 1.96025,in both cases represented by the allergen Avena Sativa accession code Q09114, you will find that the process described on page 7, step a-d have had an efficacy rate of 98 percent. Table 6 Accession Sample Sample Sample Sample Average control 03N 04N 07N 08N Q09114 1.783 2.216 1.804 2.038 1.96025 Accession Sample Sample Sample Sample Average depleted 01D 02D 05D 06D Q09114 0.071 0.038 0.042 0.008 0.03975 In table 7 you will find a similar calculation on all investigated peptides and their remaining – not yet depleted peptides - percentage. Although, looking for potentially pathogenic peptides responsible for an adverse immunologically mediated reaction to CD patients, concentration on the specific allergenic organism Avena Sativa accession Q09114.1, Officially classified to cause allergenic reactions in humans (Figure 5), is now a priority. In a systematic review on tolerable levels of gluten for people with coeliac disease conducted by Coeliac UK 2006, project code T07048, the review indicated that a daily consumption of 20 mg or more of gluten clearly induced gut mucosal abnormalities. In two studies, the ingestion of an average of 34 - 36 mg gluten daily, did not cause histological changes or clinical symptoms, but in a further study, a much smaller dose of gluten (1.5 mg daily) triggered CD symptoms. The effect of the consumption of ‘gluten-free’ products with different degrees of gluten contamination was also inconsistent between studies. Whilst some people tolerated current Codex standard ‘gluten-free’ products (less than 20 mg a day), others developed histological abnormalities whilst consuming the same products. The researchers considered that it is likely that it is the total amount of gluten ingested over time rather than the concentration of gluten in the food product that is important. The researchers concluded that there was some evidence that the current Codex standard on the situation of 20 mg gluten in gluten-free foods is not sufficiently protective for all people with coeliac disease and so there may be a case for lowering this. This study was conducted by Coeliac UK, Sept 1, 2006. Project code: T07048. In summary it turns out to be a question for the Food industry, how to organize a chain of well approved actions hindering pathogenic peptides from entering the food chain at all. New technology for a safe and effective separation of prolamins is therefore one important strategy. Efforts to improve any developed technology in favour of Nutriments without any trace of pathogenicity is therefore important. Food allergens are food substances (often proteins) that commonly cause allergic reactions or other hypersensitivity reactions. Accredited analyses on nitrogen, specific amino acids and peptides confirm a significant reduction of the suspected prolamin peptide (Avena Sativa). The total protein- and aminoacid results confirm a reduction of proteins in the depletion group corresponding to 22 percent. Whereas the proteomic laboratories have been able to prove a 98 percentage reduction of Avena Sativa pathogens. Table 7 Protein Remaining Accession amount in kDa Code wt% of the original content Q09114 2 wt% 21.0 3 wt% 20.4 L0L4J1 L0L6J0 3 wt% 32.8 L0L5H3 3 wt% 25.5 Q2EPY2 3 wt% 21.4 L0L5I0 3 wt% 22.9 I4EP88 4 wt% 26.5 L0L5H5 3 wt% 24.2 L0L5G8 5 wt% 27.8 L0L6K1 3 wt% 25.5 Q09072 6 wt% 25.7 Q09071 9 wt% 20.4 L0L6J7 9 wt% 20.4 L0L837 11 wt% 21.4 L0L8A4 11 wt% 21.3 L0L8A0 11 wt% 21.4 The identified peptides in the depleted and the control oat samples were quantified and compared to find differently expressed peptides and corresponding number of of proteins, based on data published by Greg Tanner et al Front Nutr. 2019 Oct 15:6162. Protein identification and quantification were performed using Proteome Discoverer ver. 2.4 (Thermos Fisher Scientific) against the oat database Glurp v5.0 (Ref M. Daly et al, Front Nutra. 2020 Jul 17:7:87. Doi: 10.3389) using Sequent with peptide tolerance of 5 ppm and fragment ion tolerance of 0.6 Da. Chymotrypsin was selected as enzyme and peptides were accepted with four missed cleavages. Methionine and proline oxidation and N-terminal Gln to pyro-Glu were set as variable modification, cysteine Carbamidomethyl and Tetro reagent modification on lysine and peptide N-terminus as fixed modifications. The Percolator algorithm was used for peptide spectrum match (PSM) validation with the strict false discovery rate (FDR) threshold of 1%. The TMT reporter ions were identified with 3 mum mass tolerance and without normalization. Only peptide sequences with a minimum SPS match of 65% and an average signal-to-noise ratio S / N > 10 was considered for quantification. For protein quantification unique and razor peptides were used and proteins were grouped by sharing the same sequences to minimize redundancy. The Protein abundance ratios were calculated using the average abundance of all samples. To estimate the depletion in percentage, the average abundance of depleted samples was tested by the heat map technology. The depletion is expressed as the remaining amount in wt%. The remaining amount of the potentially problematic Avena Sativa proteins are presented in table 7. Results Global quantitative proteomic analysis identified a total of 312 peptides when matched against the Oat GluProv5.1 database, with 253 peptides considered for quantitative evaluation (supplementary 1). These peptides correspond to 21 quantified proteins or protein groups of which 17 were assessable. For an overall assessment of similarities and differences in peptide profiles between depleted and control (zero) samples, Principal Component Analysis (PCA) was performed. The results are shown in fig 3. Depleted samples and control (zero) sample clustered separately in the PCA plot. The first and second component segregate the two groups account for 93% and 4% of the variability, respectively. Three of the depleted samples grouped tightly together and the fourth sample (sample 06D) was even further separated from the control (zero) samples. The control (zero) samples grouped two and two but are well separated from the depleted samples in the PCA plot. The PCA plot for the peptides and proteins correlated well as expected. Statistical analysis of the quantified peptides revealed 237 differentially expressed peptides (red in volcano plot, fig 4). All these peptides were significantly down regulated in the depleted samples compared to control (zero) samples. Only four peptides were found not statistically down regulated. However, these peptides belong to protein / proteins groups where their other peptides were significantly down regulated. Thus, these protein / proteins groups are considered as down regulated in depleted samples. Twelve of the peptides were detected in the group of control (zero) samples but in only few or absent in depleted samples. Statistical analysis of the proteins visualized in the volcano plot shows 16 down regulated proteins out of the 21 quantified proteins. To estimate the depletion of the avenin proteins, the average abundance of depleted samples was divided by the average abundance of control (zero) samples. The depletion for the differentially expressed proteins was estimated to range from 2 wt% to 11 wt%, with exception for one protein where depletion was estimated to 21 wt%. The depletion is expressed as the remaining wt% of the original content.

Claims

Claims 1. A method for treatment of oat, said method comprising the sequential steps of: a. providing oat kernels, b. heat treating the oat kernels in a temperature in the interval 95 - 100 °C, c. processing the oat kernels in a disc mill with discs, to obtain milled oat kernels, d. subjecting the milled oat kernels to a separation with respect to size to obtain at least one finer product fraction and at least one coarser fraction.

2. The method according to claim 1, wherein the amount of at least some proteins and / or peptides known to cause dietary sensitivities and disorders in some individuals in the at least one finer product fraction is reduced compared to the oat kernels provided in step a).

3. The method according to any one of claims 1-2, wherein the heat treating in step b) is hydrothermal.

4. The method according to any one of claims 1-3, wherein the heat treating in step b) is carried out in a process vessel at atmospheric pressure by supplying steam until the temperature throughout the entire vessel has reached at least 95 °C, preferably at least 99 °C, whereby the treatment is continued for a period of time in the interval 20-60 minutes.

5. The method according to any one of claims 1-4, wherein a drying step is performed between steps b) and c), wherein the drying step comprises supplying heated air to the treated oat kernels from step b), and which drying step is performed at a temperature below 70 °C.

6. The method according to claim 5, wherein the drying step is carried out until the water content in the treated oat kernels is below 15 wt%, preferably below 14 wt%, more preferably below 13 wt%, most preferably below 12 wt%.

7. The method according to any one of claims 1-6, wherein the disc mill in step c) has a distance between the discs in the range 0.60 to 1.20 mm, preferably 0.70 to 1.10 mm.

8. The method according to any one of claims 1-7, wherein a rotation direction of the disc mill in step c) can be alternated.

9. The method according to any one of claims 1-8, wherein the separation in step d) is performed with a sift.

10. The method according to any one of claims 1-9, wherein the separation in step d) is performed with a sift with a nominal aperture size in the interval 430 – 830 µm according to ASTM E11.

11. The method according to any one of claims 1-10, wherein the separation in step d) is performed in more than one step with at least two or more different sifts.

12. The method according to any one of claims 1-11, wherein the separation in step d) is first performed with a first sift with a nominal aperture size in the interval 430 – 800 µm according to ASTM E11 and subsequently a second sift with a nominal aperture size in the interval 801 – 1200 µm according to ASTM E11.

13. The method according to any one of claims 1-12, wherein the at least one finer product fraction is recovered and used in food or feed.

14. The method according to any one of claims 1-13, wherein the at least one coarser fraction is recovered and used in food or feed.

15. The method according to any one of claims 1-14, wherein the at least one coarser fraction is recovered and subjected to at least one further separation step to enrich at least β-glucan.

16. An oat flour wherein the amount of each of the proteins with accession numbers Q09114, L0L4J1, L0L6J0, L0L5H3, Q2EPY2, L0L5I0, I4EP88, L0L5H5, L0L5G8, L0L6K1, Q09072, Q09071, L0L6J7, L0L837, L0L8A4, and L0L8A0 from Avena Sativa are reduced with at least 50 wt%.

17. The oat flour according to claim 16, wherein the oat flour has a water holding capacity of less than 0.8 ml / g product as measured according to I. Jokinen et al. in LWT Vol.163, 15 June 2022.

18. The oat flour according to any one of claims 16-17, wherein the amount of the protein with accession code Q09114, has been reduced with at least 90 wt%, preferably at least 95 wt%, more preferably at least 98 wt%, compared to the original oat.

19. The oat flour according to any one of claims 16-18, wherein the oat flour is at least one finer product fraction manufactured according to any one of claims 1-15.

20. A nutriment, which nutrient is made with at least one ingredient, which at least one ingredient comprises an oat flour according to any one of claims 16-19.

21. The nutriment according to claim 20, wherein the nutriment is a food and wherein at least 52 wt% of all ingredients are the at least one finer product fraction finer according to the method of any one of claims 1-16.

22. The nutriment according to any one of claims 20-21, wherein the nutriment is bread.

23. The nutriment according to claim 22, wherein the bread has a porosity which is larger than 40%.

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