WO2008090126A1 - Boissons pour patients cœliaques et personnes sensibles au gluten/à la gliadine et leur procédé de fabrication - Google Patents

Boissons pour patients cœliaques et personnes sensibles au gluten/à la gliadine et leur procédé de fabrication Download PDF

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WO2008090126A1
WO2008090126A1 PCT/EP2008/050647 EP2008050647W WO2008090126A1 WO 2008090126 A1 WO2008090126 A1 WO 2008090126A1 EP 2008050647 W EP2008050647 W EP 2008050647W WO 2008090126 A1 WO2008090126 A1 WO 2008090126A1
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beverage
fragments
enzymes
prolamine
beer
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PCT/EP2008/050647
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German (de)
English (en)
Inventor
Stefan Marx
Jens Otterbach-Noä
Olaf Langer
Jens Zotzel
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N-Zyme Biotec Gmbh
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Publication of WO2008090126A1 publication Critical patent/WO2008090126A1/fr

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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12C—BEER; PREPARATION OF BEER BY FERMENTATION; PREPARATION OF MALT FOR MAKING BEER; PREPARATION OF HOPS FOR MAKING BEER
    • C12C12/00—Processes specially adapted for making special kinds of beer
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
    • A23C9/00—Milk preparations; Milk powder or milk powder preparations
    • A23C9/12—Fermented milk preparations; Treatment using microorganisms or enzymes
    • A23C9/1203—Addition of, or treatment with, enzymes or microorganisms other than lactobacteriaceae
    • A23C9/1216—Other enzymes
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Their preparation
    • A23L2/70—Clarifying or fining of non-alcoholic beverages; Removing unwanted matter
    • A23L2/84—Clarifying or fining of non-alcoholic beverages; Removing unwanted matter using microorganisms or biological material, e.g. enzymes
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L5/00—Preparation or treatment of foods or foodstuffs, in general; Food or foodstuffs obtained thereby; Materials therefor
    • A23L5/20—Removal of unwanted matter, e.g. deodorisation or detoxification
    • A23L5/25—Removal of unwanted matter, e.g. deodorisation or detoxification using enzymes
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12C—BEER; PREPARATION OF BEER BY FERMENTATION; PREPARATION OF MALT FOR MAKING BEER; PREPARATION OF HOPS FOR MAKING BEER
    • C12C5/00—Other raw materials for the preparation of beer
    • C12C5/004—Enzymes
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12C—BEER; PREPARATION OF BEER BY FERMENTATION; PREPARATION OF MALT FOR MAKING BEER; PREPARATION OF HOPS FOR MAKING BEER
    • C12C5/00—Other raw materials for the preparation of beer
    • C12C5/02—Additives for beer
    • C12C5/023—Additives for beer enhancing the vitamin content
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12H—PASTEURISATION, STERILISATION, PRESERVATION, PURIFICATION, CLARIFICATION OR AGEING OF ALCOHOLIC BEVERAGES; METHODS FOR ALTERING THE ALCOHOL CONTENT OF FERMENTED SOLUTIONS OR ALCOHOLIC BEVERAGES
    • C12H1/00—Pasteurisation, sterilisation, preservation, purification, clarification, or ageing of alcoholic beverages
    • C12H1/02—Pasteurisation, sterilisation, preservation, purification, clarification, or ageing of alcoholic beverages combined with removal of precipitate or added materials, e.g. adsorption material
    • C12H1/04—Pasteurisation, sterilisation, preservation, purification, clarification, or ageing of alcoholic beverages combined with removal of precipitate or added materials, e.g. adsorption material with the aid of ion-exchange material or inert clarification material, e.g. adsorption material
    • C12H1/0408—Pasteurisation, sterilisation, preservation, purification, clarification, or ageing of alcoholic beverages combined with removal of precipitate or added materials, e.g. adsorption material with the aid of ion-exchange material or inert clarification material, e.g. adsorption material with the aid of inorganic added material
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
    • C12Y101/03—Oxidoreductases acting on the CH-OH group of donors (1.1) with a oxygen as acceptor (1.1.3)
    • C12Y101/03005—Hexose oxidase (1.1.3.5)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y110/00—Oxidoreductases acting on diphenols and related substances as donors (1.10)
    • C12Y110/03—Oxidoreductases acting on diphenols and related substances as donors (1.10) with an oxygen as acceptor (1.10.3)
    • C12Y110/03002—Laccase (1.10.3.2)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y111/00—Oxidoreductases acting on a peroxide as acceptor (1.11)
    • C12Y111/01—Peroxidases (1.11.1)
    • C12Y111/01007—Peroxidase (1.11.1.7), i.e. horseradish-peroxidase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y114/00—Oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (1.14)
    • C12Y114/18—Oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (1.14) with another compound as one donor, and incorporation of one atom of oxygen (1.14.18)
    • C12Y114/18001—Tyrosinase (1.14.18.1)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y203/00—Acyltransferases (2.3)
    • C12Y203/02—Aminoacyltransferases (2.3.2)
    • C12Y203/02013—Protein-glutamine gamma-glutamyltransferase (2.3.2.13), i.e. transglutaminase or factor XIII
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y503/00—Intramolecular oxidoreductases (5.3)
    • C12Y503/04—Intramolecular oxidoreductases (5.3) transposing S-S bonds (5.3.4)
    • C12Y503/04001—Protein disulfide-isomerase (5.3.4.1), i.e. disufide bond-forming enzyme

Definitions

  • the present invention relates to beverages for celiac patients and gluten / gliadin-sensitive persons and to processes for their preparation.
  • Prolamins are a heterogeneous group of ethanol-soluble proteins of various cereals and are referred to as gliadins in wheat, as hordeins in barley, as secalines in rye and as avensins in oats. Despite structural differences within the primary sequence, the prolamins, whether derived from wheat or other cereals, are also commonly referred to as glutins or gliadins.
  • a large number of cereals used in the food and beverage industry contain Prolamine in z.T. considerable quantities. Examples of the beverage industry are: all types of beer and mixed beer beverages, malt-based soft drinks (e.g., malt beer), corn or cereal coffee.
  • Celiac disease or sprue is a chronic autoimmune disease that is triggered in genetically predisposed patients by certain cereal proteins (prolamins, gluten).
  • celiac disease patients intestinal malabsorption syndromes usually occur as early as the first or second year of life as a result of extensive lesions of the small intestine mucosa caused by the action of gluten.
  • the vast majority of patients express so-called HLA-DQ2 and / or HLA-DQ8 molecules.
  • HLA-DQ2 and / or HLA-DQ8 molecules The current scientific opinion assumes that interaction of specific gliadin molecules with HLA DQ2 / HLA-DQ8 antigens the proliferation of T lymphocytes is induced. This excessive immune response is causally related to the degeneration of the small intestinal mucosa.
  • Patients with Duhring's disease also have celiac disease in up to 24% of cases, although typical symptoms of the latter can often be absent.
  • In small bowel biopsies up to 85% of dermatitis herpeticiformis patients have celiac disease-specific changes with variable villus atrophy.
  • Patients with Dermatitis herpetiformis Duhring should therefore be tested for celiac disease. In such cases, the gluten-free diet usually leads in the long term to the disappearance of the skin lesions.
  • Gliadin / gluten sensitivity is known as mini-celiac disease and has been reported in more than 90% of the white Anglo-Saxon population with neurodegenerative diseases (Fajcsak (2002) FDP- health & nutrition today, The world of food ingredients 09: 75-82).
  • the selection and cultivation of food grain has been based on a high protein and thus also gluten content for two reasons:
  • Protein is the most nutritionally-phy- siological component of starch and other polysaccharides, and gluten is crucial for certain technological properties in cereal processing.
  • the content and the structure of the adhesive determine the essential physico-chemical properties such as elasticity, gas retention, stickiness or fermentation stability of doughs.
  • gliadins are also present in the product, and in quantities that prohibit consumption by celiac disease patients.
  • gliadin-free cereals buckwheat, rice, millet, etc.
  • these drinks usually also have altered organoleptic properties such as taste or mouthfeel.
  • organoleptic properties such as taste or mouthfeel.
  • Physicochemical properties, such as foam formation and foam stability usually do not match those of traditional products expected by the consumer.
  • EP 0 949 329 A1 describes a gluten-free beer brewed from buckwheat and hydrolyzed cornstarch using amylolytic enzymes and glucanase.
  • the published patent application DE 10 2004 037 696 likewise describes a process for producing a gliadin-free beer using gluten-free raw materials and an enzyme feed for liquefaction or saccharification of mash.
  • Crosslinking enzymes are enzymes that can generate covalent bonds within proteins or between proteins and other substances such as carbohydrates and phenols, thus causing the formation of protein aggregates, possibly with the participation of other substances.
  • Typical representatives are transglutaminases, peroxidases, hexose oxidases, Tyrosinases and laccases, see also Thalmann CR & Lötzbeyer T 2002: Enzyme cross-linking of proteins with tyrosinase. Eur. Food Res. Technol. 214: 276-281; Boeriu CG, Oudgenoeg G, Spekking WT, Berendsen LB, Vancon L, Boumans H, Groups H, van Berkel WJ, Laane. US Pat.
  • Transglutaminases protein glutamine: amine ⁇ -glutamyltransferase, E.C. 2.3.2.13 catalyze the construction of stable cross-links between proteins.
  • the ⁇ -carboxyamide function of glutamine side chains is transferred to the ⁇ -amino group of lysine residues with the release of ammonium ions (FoIk and Finlayson, Adv. Protein Chem. 31, 1-133 (1977)).
  • the bacterial transglutaminase of Streptomyces mobaraensis, Streptomyces hygroscopius and Streptomyces fradiae is particularly suitable.
  • the bacterial transglutaminase is derived from the non-pathogenic and non-toxic Streptomyces mobaraensis. This TGase preparation has been classified by the Food and Drug Administration (FDA) as Generally Recognized as Safe (GRAS) (GRN 000095).
  • FDA Food and Drug Administration
  • GRAS Generally Recognized as Safe
  • Examples include: Crosslinking of meat, fish, cheese, milk, whey proteins, soy proteins and wheat proteins to achieve an improved structure, a higher viscosity or a pleasant mouthfeel.
  • WO 02/051873 describes a process for obtaining purified starch from proteinaceous vegetable raw materials by the action of cross-linking agents, e.g. Transglutaminase. After cross-linking of the proteins occurring in the raw material or additionally added by transglutaminase, a facilitated separation of the starch from the protein network is possible.
  • cross-linking agents e.g. Transglutaminase
  • EP 1 190 624 A2 describes methods for improving the baking technology quality of low-wheat doughs by means of transglutaminase. Due to the use of enzymes u.a. an increased gas-holding capacity, a lower dough stickiness and an improved fermentation stability can be achieved.
  • US 6,106,887 discloses a process for producing modified cereal flours using transglutaminase during the tempering and / or milling process.
  • EP 0 760 209 A1 discloses the use of transglutaminase for producing bakery products with a multilayer structure.
  • WO 01/65948 discloses protein preparation prepared from the action of transglutaminase from wheat protein and whey protein having improved technological properties such as emulsifying ability, gelling ability or water binding capacity.
  • WO 2006/051093 describes a process for the preparation of prolamine-reduced beverages by modification of the prolamins by means of transglutaminase and subsequent removal of the prolamines modified in this way.
  • prolactin levels below 20 ppm could be achieved.
  • these products, as well as other products with prolactin content ⁇ 20 ppm can continue to cause disease in celiac patients.
  • the object of the present invention was to overcome the stated disadvantages and problems of the prior art, in particular to provide a method for producing beverages which are suitable for celiac patients and gluten / gliadin-sensitive persons, and related products.
  • the object is achieved by a method for producing a beverage, a beverage base, a beverage concentrate or a beverage additive with a reduced content of prolamine fragments from prolaminhalti- gene raw materials with the following steps:
  • Cereals such as wheat, rye, oats, barley, spelled, green wheat, einkorn, emmer, triticale, bulgur, kamut or mixtures thereof are particularly suitable as prolamin-containing raw materials.
  • Suitable crosslinking enzymes are, in particular, those from the enzyme classes of transglutaminases (EC 2.3.2.13), peroxidases (EC 1.11.1.7), hexose oxidases (EC 1.1.3.5), tyrosinases (EC 1.14.18.1), laccases (EC 1.10.3.2), protein disulfide isomerases (EC 5.3.4.1) and combinations thereof.
  • a particularly preferred cross-linking enzyme are bacterial transglutaminases, in particular Ca 2+ -independent transglutaminases from Streptomyces mobaraensis.
  • prolamins are ethanol-soluble proteins from cereal species, which are also referred to as gluten, gluten, gliadins, hordeins, secalines or avensins.
  • Prolamine fragments are fragments of prolamins that can be found in beverages and that respond to celiac and gluten / and gliadin-sensitive individuals with symptoms.
  • the prolamine fragments can be formed by the activity of malzsten enzymes, the use of enzymes during production or by enzymes formed by added microorganisms.
  • the term “prolamine fragments” is synonymous with the term “peptides potentially toxic to celiac disease patients”.
  • ELISA 2 For the quantification of the prolamine fragments, a competitive ELISA ("ELISA 2") specified for prolamin fragments is available (r-Biopharm, Darmstadt). "Drink” means a food that can be consumed in liquid form.
  • “Beverage base” or “beverage concentrate” means a precursor for producing a foodstuff in solid or liquid form that can be consumed as food after further processing.
  • the inventive method the content of Prolaminfragmen- th in the drinks, beverage concentrates or beverage precursors can be reduced, the physico-chemical properties of the beverage are as little as possible changed.
  • the content of prolamine fragments is reduced by at least 50%, preferably by at least 80%, more preferably by at least 90%.
  • the treatment with transglutaminase according to the invention can be used for the production of beers whose organoleptic and physico-chemical properties correspond to those of conventional beers. This applies in particular to foaming behavior and foam stability, density, color, extract content, degree of fermentation or bitterness units.
  • the amount of enzyme to be used depends on the enzyme preparation and can vary within wide limits. It depends on the proliferous content of the raw materials and intermediates used, the reaction time, reaction temperature, pH, etc., as known to those skilled in the art of dealing with enzymes.
  • beverages can be produced which are selected from the group consisting of alcoholic beer, alcohol-reduced beer, non-alcoholic beer, malt beer, beer mixed drinks, lemonades, soft drinks, fruit juice drinks, emulsion drinks, fruit juice mixed drinks and mixtures thereof.
  • vegetable or microbial proteins may be added to the beverage or precursor of the beverage before, during or after contact with the crosslinking enzymes for food-approved proteins and protein hydrolysates such as gelatin, milk and whey proteins.
  • all compounds which function as amine donors for example lysine-rich peptides
  • are accepted by the crosslinking enzymes as substrates are suitable as further ingredients, so that the prolamine fragments can be bound to corresponding substrates.
  • immobilized substrates are added so that the prolamine fragments are bound by the cross-linking enzymes to these immobilized substrates.
  • This binding to the solid phase (matrix) improves the efficiency of the reaction and significantly facilitates the removal of prolamine fragments.
  • an adsorption step is carried out to remove the modified prolamine fragments. Filtration of silica, in particular amorphous silica such as kieselguhr, has proven particularly suitable. Depending on the process, kieselguhr filtration may also be the only step to remove the modified prolamine fragments.
  • the transglutaminase is also removed from the beverage, so that processes for inactivating the enzyme can be made significantly more product-friendly, since no or only a slight temperature effect is necessary for inactivating the enzyme activity.
  • the enzymes can be used in purified form or in the form of a preparation, e.g. an extract from a food-compatible organism.
  • contacting with crosslinking enzymes can be accomplished by adding microorganisms that produce recombinant cross-linking enzymes.
  • microorganisms yeasts are particularly suitable.
  • recombinant cross-linking enzymes are already expressed in the cereals, which then come into contact with the prolamine fragments in the course of the process.
  • the transglutaminase is bound to a solid phase, for example to polymeric carriers, silica gels such as kieselguhr, bentonite or silica sol.
  • a solid phase for example to polymeric carriers, silica gels such as kieselguhr, bentonite or silica sol.
  • Such solid phase-bound transglutaminases are particularly easy to remove during the separation steps.
  • the selection of the process conditions can be determined in accordance with the manufacturing process by a person skilled in the art. It is known to the person skilled in the art that the reaction rate of an enzyme reaction generally increases with the amount of enzymes and the temperature. Low Temperatures require higher amounts or longer reaction times. At higher temperatures, lower quantities or shorter reaction times suffice.
  • contacting with the beverage or beverage precursor and crosslinking enzymes occurs for a period of between 10 minutes and 72 hours.
  • the temperature is between 0 and 60 ° C.
  • the contacting is followed by an inactivation step of the enzymes, in particular a heat treatment.
  • Another object of the invention is a beverage, beverage base, beverage concentrate or beverage additive obtainable by the inventive method and a food containing the beverage base or the beverage concentrate, for example in the form of a yogurt, a milk mix beverage or a dietary beverage with cereal portions, or a beverage powder.
  • the process reduces the content of prolamine and prolamine fragments of the beverage.
  • the prolactin content after treatment using ELISA 1 is below 200 ppm, more preferably below 100 ppm, even more preferably below 50 ppm, and most preferably below 20 ppm.
  • the content of prolamine fragments using ELISA 2 is preferably below 2000 ppm, more preferably below 1500 ppm, even more preferably below 1200 ppm, and most preferably within the detection limit of the test method.
  • the detection limit for Elisa 2 determined on specified gluten-free foods is 922 ppm (as of August 2006).
  • a drink is obtained, which due to the reduced prolactin content better compatibility for patients with Zö- liakie, dermatitis herpetiformis or gluten / gliadin sensitivity.
  • corresponding drinks also have improved physiological properties, in particular with regard to turbidity stability (colloidal stability).
  • Celiac patients should be supplemented with calcium, with a daily dose of at least 1200 mg (Pazianas et al 2005, Osteoporos Int., 16: 56-63).
  • Many cereal-based gluten-free products (rice, corn, etc.) contain significantly lower levels of thiamine, riboflavin or niacin compared to standard wheat products.
  • the use of highly processed, non-fortified cereal-based gluten-free products may result in malnutrition of the vitamins thiamine, riboflavin or niacin (Thompson 1999, J. Am. Diet. Assoc. 99: 858-862).
  • 30 contained less folate than the comparable standard products.
  • the drink according to the invention can also be useful for the celiac disease patient to improve the situation with regard to vital substances.
  • the following table shows a selection of vital signs Substances whose average contents are contained in a Pilsener beer (Selected chapters of brewery technology, W. Back (Ed.), ausverlag Hans Carl, Nuremberg, 20005) and daily doses recommended by the DGE (2004).
  • the drink according to the invention may additionally be enriched with minerals, vitamins, trace elements.
  • contents which are higher than the naturally occurring contents of such substances are particularly suitable.
  • the levels can be determined according to international recommendations for use (daily intake) for food including dietetic foods and do not exceed the requirements of European food legislation.
  • Figure 1 shows the calibration curve of a RIDASCREEN ® Gliadin competitive as- says.
  • FIG. 2 shows the removal of prolamine and prolamine fragments from beer by using immobilized or soluble transglutaminase.
  • FIG. 3 shows the transglutaminase activity in the filtrate after treatment with diatomaceous earth in various diatomaceous earth concentrations.
  • FIG. 4 shows the determination of the transglutaminase concentration after filtration with diatomaceous earth (lane M: MV marker, lane 1: before filtration, lane 2: 5 g of silica gel / l, lane 3: 10 g of kieselguhr / l, lane 4: 25 g Kieselguhr / l, Lane 5: 50 g kieselguhr / l, Lane 6: 100 g kieselguhr / l, Lane 7: 50 ng BSA, Lane 8: 25 ng BSA, Lane 9: 10 ng BSA).
  • FIG. 5 shows the transglutaminase activity in beer after treatment with kieselguhr and filtration.
  • FIG. 6 shows an overview of the content of toxic peptides in different types of beer.
  • the analytical detection of prolamine fragments in raw materials, intermediates and final drinks was carried out with the RIDASCREEN ® gliadin competitive test, a competitive enzyme immunoassay for the quantitative determination of peptide sequences of prolamins from wheat (gliadin), rye (secalin) and barley (hordein) in food.
  • the monoclonal antibody R5 used recognizes, inter alia, the toxic sequence QQPFP, which occurs repeatedly in prolamins.
  • the PFP motif to which the R5 antibody binds occurs repeatedly in small peptides toxic to celiac disease patients (see Kahlenberg et al., Proceedings of the 18th Meeting of the Working Group on Prolamin Analysis Toxicity, published by Scientific Scripts).
  • the test principle is based on an antigen-antibody reaction.
  • the wells of the microtiter strips are coated with gliadin as the antigen.
  • Glialin standards calibrated against the QQPFP peptide or sample to be analyzed, and anti-gliadin antibodies (monoclonal R5 antibody) coupled to peroxidase are added simultaneously.
  • the labeled antibodies (enzyme conjugate) bind to gliadin of the microtiter plate and the prolamin peptides in the sample solution.
  • bound enzyme conjugate in the solution is removed which remains conjugate to the microtiter plate.
  • Detection is carried out by adding the substrate urea peroxide and a chromogen (tetramethylbenzidine).
  • the antibody bound to the antibody converts the colorless chromogen into a blue end product.
  • the addition of a stop reagent (H 2 SO 4 ) leads to a color change from blue to yellow.
  • the measurement is carried out photometrically at 450 nm in a microtiter plate reader.
  • the QQPPP concentration in ⁇ g / g (ppm) corresponding to the absorbance at 450 nm of the sample is read from the calibration curve and from this the actual QQPFP content of the sample is calculated.
  • transglutaminase formulation 1 g was dissolved in 1000 ml of an acetic acid / acetate buffer (pH 4.6). After adding diatomaceous earth, it was stirred for 15 minutes and then filtered through a fluted filter. Non-kieselguhr bound transglutaminase was removed by washing with cold beer several times. 1 g of the transglutaminase-coupled kieseigur were added to 1000 ml of beer. With constant stirring, the suspension was incubated at 5 ° C. After completion of the reaction, undissolved constituents were filtered through a pleated filter. The concentration of toxic peptides was determined in the filtrate (see Example 1).
  • the transglutaminase concentration is calculated to be ⁇ 0.8 mg / l (see FIG. 4).
  • the contaminants present in the transglutaminase preparation are also removed by the method described.
  • transglutaminase activity in the filtrate was determined (FIG. 5).

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Abstract

L'invention concerne un procédé de fabrication d'une boisson, d'une substance de base de boisson, d'un concentré de boisson ou d'un additif pour boisson présentant une teneur réduite en fragments de prolamine provenant de matières premières contenant de la prolamine. Le procédé comprend les étapes suivantes : a) mise en contact de la boisson ou d'une phase préalable de la boisson avec des enzymes à réticulation transversale, de manière à obtenir des fragments de prolamine modifiés, b) élimination au moins partielle des fragments de prolamine modifiés.
PCT/EP2008/050647 2007-01-22 2008-01-21 Boissons pour patients cœliaques et personnes sensibles au gluten/à la gliadine et leur procédé de fabrication WO2008090126A1 (fr)

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EP07100904 2007-01-22

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DE102020117175A1 (de) 2020-06-30 2021-12-30 Krombacher Brauerei Bernhard Schadeberg GmbH & Co. KG Verfahren zum Behandeln eines Bieres, Verfahren zum Herstellen eines glutenfreien Bieres, Bier und entsprechende Verwendung

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Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE102020117175A1 (de) 2020-06-30 2021-12-30 Krombacher Brauerei Bernhard Schadeberg GmbH & Co. KG Verfahren zum Behandeln eines Bieres, Verfahren zum Herstellen eines glutenfreien Bieres, Bier und entsprechende Verwendung
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CN112121019A (zh) * 2020-09-23 2020-12-25 合肥工业大学 抗氧化型淀粉基糊精复合纳米颗粒及其制备方法与应用
CN112121019B (zh) * 2020-09-23 2022-05-31 合肥工业大学 抗氧化型淀粉基糊精复合纳米颗粒及其制备方法与应用

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