EP3071041A1 - Verfahren zur herstellung halbfertiger nahrungsmittelprodukte auf mehlbasis mit trans-glutaminase-aktivität und einer lysinquelle - Google Patents
Verfahren zur herstellung halbfertiger nahrungsmittelprodukte auf mehlbasis mit trans-glutaminase-aktivität und einer lysinquelleInfo
- Publication number
- EP3071041A1 EP3071041A1 EP14798966.9A EP14798966A EP3071041A1 EP 3071041 A1 EP3071041 A1 EP 3071041A1 EP 14798966 A EP14798966 A EP 14798966A EP 3071041 A1 EP3071041 A1 EP 3071041A1
- Authority
- EP
- European Patent Office
- Prior art keywords
- spp
- lysine
- process according
- source
- gluten
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
Links
- 235000013312 flour Nutrition 0.000 title claims abstract description 44
- 238000000034 method Methods 0.000 title claims abstract description 39
- 230000008569 process Effects 0.000 title claims abstract description 35
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 title claims abstract description 30
- 239000004472 Lysine Substances 0.000 title claims abstract description 30
- 235000013305 food Nutrition 0.000 title claims abstract description 24
- 230000000694 effects Effects 0.000 title claims abstract description 16
- 238000002360 preparation method Methods 0.000 title claims abstract description 16
- 108010068370 Glutens Proteins 0.000 claims abstract description 41
- 235000021312 gluten Nutrition 0.000 claims abstract description 37
- 108060008539 Transglutaminase Proteins 0.000 claims abstract description 26
- 102000003601 transglutaminase Human genes 0.000 claims abstract description 26
- 238000011282 treatment Methods 0.000 claims abstract description 19
- 235000013311 vegetables Nutrition 0.000 claims abstract description 10
- 230000000890 antigenic effect Effects 0.000 claims abstract description 9
- 238000007056 transamidation reaction Methods 0.000 claims abstract description 6
- 230000009471 action Effects 0.000 claims abstract description 5
- 229930014626 natural product Natural products 0.000 claims abstract description 5
- 239000013592 cell lysate Substances 0.000 claims abstract description 3
- 244000005700 microbiome Species 0.000 claims description 14
- 239000006166 lysate Substances 0.000 claims description 13
- 239000006228 supernatant Substances 0.000 claims description 9
- 210000002421 cell wall Anatomy 0.000 claims description 8
- 239000011265 semifinished product Substances 0.000 claims description 8
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 claims description 6
- 102000004190 Enzymes Human genes 0.000 claims description 5
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- 238000005119 centrifugation Methods 0.000 claims description 5
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- 229940039696 lactobacillus Drugs 0.000 claims description 5
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- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 claims description 4
- 241000235070 Saccharomyces Species 0.000 claims description 4
- WPYMKLBDIGXBTP-UHFFFAOYSA-N benzoic acid Chemical compound OC(=O)C1=CC=CC=C1 WPYMKLBDIGXBTP-UHFFFAOYSA-N 0.000 claims description 4
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- 229940082787 spirulina Drugs 0.000 claims description 3
- PWKSKIMOESPYIA-UHFFFAOYSA-N 2-acetamido-3-sulfanylpropanoic acid Chemical compound CC(=O)NC(CS)C(O)=O PWKSKIMOESPYIA-UHFFFAOYSA-N 0.000 claims description 2
- 241000187844 Actinoplanes Species 0.000 claims description 2
- 241000193830 Bacillus <bacterium> Species 0.000 claims description 2
- 239000005711 Benzoic acid Substances 0.000 claims description 2
- 241000206594 Carnobacterium Species 0.000 claims description 2
- 102000012286 Chitinases Human genes 0.000 claims description 2
- 108010022172 Chitinases Proteins 0.000 claims description 2
- FEWJPZIEWOKRBE-JCYAYHJZSA-N Dextrotartaric acid Chemical compound OC(=O)[C@H](O)[C@@H](O)C(O)=O FEWJPZIEWOKRBE-JCYAYHJZSA-N 0.000 claims description 2
- 108010022769 Glucan 1,3-beta-Glucosidase Proteins 0.000 claims description 2
- 241000205062 Halobacterium Species 0.000 claims description 2
- 241000235649 Kluyveromyces Species 0.000 claims description 2
- NVNLLIYOARQCIX-MSHCCFNRSA-N Nisin Chemical compound N1C(=O)[C@@H](CC(C)C)NC(=O)C(=C)NC(=O)[C@@H]([C@H](C)CC)NC(=O)[C@@H](NC(=O)C(=C/C)/NC(=O)[C@H](N)[C@H](C)CC)CSC[C@@H]1C(=O)N[C@@H]1C(=O)N2CCC[C@@H]2C(=O)NCC(=O)N[C@@H](C(=O)N[C@H](CCCCN)C(=O)N[C@@H]2C(NCC(=O)N[C@H](C)C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCSC)C(=O)NCC(=O)N[C@H](CS[C@@H]2C)C(=O)N[C@H](CC(N)=O)C(=O)N[C@H](CCSC)C(=O)N[C@H](CCCCN)C(=O)N[C@@H]2C(N[C@H](C)C(=O)N[C@@H]3C(=O)N[C@@H](C(N[C@H](CC=4NC=NC=4)C(=O)N[C@H](CS[C@@H]3C)C(=O)N[C@H](CO)C(=O)N[C@H]([C@H](C)CC)C(=O)N[C@H](CC=3NC=NC=3)C(=O)N[C@H](C(C)C)C(=O)NC(=C)C(=O)N[C@H](CCCCN)C(O)=O)=O)CS[C@@H]2C)=O)=O)CS[C@@H]1C NVNLLIYOARQCIX-MSHCCFNRSA-N 0.000 claims description 2
- 108010053775 Nisin Proteins 0.000 claims description 2
- 241000191025 Rhodobacter Species 0.000 claims description 2
- 241000191940 Staphylococcus Species 0.000 claims description 2
- 241000194017 Streptococcus Species 0.000 claims description 2
- FEWJPZIEWOKRBE-UHFFFAOYSA-N Tartaric acid Natural products [H+].[H+].[O-]C(=O)C(O)C(O)C([O-])=O FEWJPZIEWOKRBE-UHFFFAOYSA-N 0.000 claims description 2
- VLSOAXRVHARBEQ-UHFFFAOYSA-N [4-fluoro-2-(hydroxymethyl)phenyl]methanol Chemical compound OCC1=CC=C(F)C=C1CO VLSOAXRVHARBEQ-UHFFFAOYSA-N 0.000 claims description 2
- NTOZOESJXIBDLD-UHFFFAOYSA-L [Ca+2].[O-]S(=O)S([O-])(=O)=O Chemical compound [Ca+2].[O-]S(=O)S([O-])(=O)=O NTOZOESJXIBDLD-UHFFFAOYSA-L 0.000 claims description 2
- 235000010323 ascorbic acid Nutrition 0.000 claims description 2
- 229960005070 ascorbic acid Drugs 0.000 claims description 2
- 239000011668 ascorbic acid Substances 0.000 claims description 2
- 235000010233 benzoic acid Nutrition 0.000 claims description 2
- 229960004365 benzoic acid Drugs 0.000 claims description 2
- 239000003638 chemical reducing agent Substances 0.000 claims description 2
- 239000003795 chemical substances by application Substances 0.000 claims description 2
- 229960004106 citric acid Drugs 0.000 claims description 2
- 235000015165 citric acid Nutrition 0.000 claims description 2
- 230000009089 cytolysis Effects 0.000 claims description 2
- BEFDCLMNVWHSGT-UHFFFAOYSA-N ethenylcyclopentane Chemical compound C=CC1CCCC1 BEFDCLMNVWHSGT-UHFFFAOYSA-N 0.000 claims description 2
- 235000011389 fruit/vegetable juice Nutrition 0.000 claims description 2
- 230000002538 fungal effect Effects 0.000 claims description 2
- 239000004309 nisin Substances 0.000 claims description 2
- 235000010297 nisin Nutrition 0.000 claims description 2
- 231100000252 nontoxic Toxicity 0.000 claims description 2
- 230000003000 nontoxic effect Effects 0.000 claims description 2
- RWPGFSMJFRPDDP-UHFFFAOYSA-L potassium metabisulfite Chemical compound [K+].[K+].[O-]S(=O)S([O-])(=O)=O RWPGFSMJFRPDDP-UHFFFAOYSA-L 0.000 claims description 2
- 229940043349 potassium metabisulfite Drugs 0.000 claims description 2
- 235000010263 potassium metabisulphite Nutrition 0.000 claims description 2
- LJPYJRMMPVFEKR-UHFFFAOYSA-N prop-2-ynylurea Chemical compound NC(=O)NCC#C LJPYJRMMPVFEKR-UHFFFAOYSA-N 0.000 claims description 2
- HRZFUMHJMZEROT-UHFFFAOYSA-L sodium disulfite Chemical compound [Na+].[Na+].[O-]S(=O)S([O-])(=O)=O HRZFUMHJMZEROT-UHFFFAOYSA-L 0.000 claims description 2
- 229940001584 sodium metabisulfite Drugs 0.000 claims description 2
- 235000010262 sodium metabisulphite Nutrition 0.000 claims description 2
- 235000010199 sorbic acid Nutrition 0.000 claims description 2
- 239000004334 sorbic acid Substances 0.000 claims description 2
- 229940075582 sorbic acid Drugs 0.000 claims description 2
- 235000002906 tartaric acid Nutrition 0.000 claims description 2
- 239000011975 tartaric acid Substances 0.000 claims description 2
- 229960001367 tartaric acid Drugs 0.000 claims description 2
- 241000894006 Bacteria Species 0.000 claims 1
- 230000003213 activating effect Effects 0.000 abstract 1
- 239000000047 product Substances 0.000 description 18
- 238000004519 manufacturing process Methods 0.000 description 7
- 208000015943 Coeliac disease Diseases 0.000 description 6
- 108010061711 Gliadin Proteins 0.000 description 5
- 239000000203 mixture Substances 0.000 description 5
- 239000012071 phase Substances 0.000 description 5
- 230000001580 bacterial effect Effects 0.000 description 4
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 3
- 230000001419 dependent effect Effects 0.000 description 3
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- 241000196324 Embryophyta Species 0.000 description 2
- QUSNBJAOOMFDIB-UHFFFAOYSA-N Ethylamine Chemical compound CCN QUSNBJAOOMFDIB-UHFFFAOYSA-N 0.000 description 2
- BAVYZALUXZFZLV-UHFFFAOYSA-N Methylamine Chemical compound NC BAVYZALUXZFZLV-UHFFFAOYSA-N 0.000 description 2
- 241000209140 Triticum Species 0.000 description 2
- 235000021307 Triticum Nutrition 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 235000015173 baked goods and baking mixes Nutrition 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
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- 238000013461 design Methods 0.000 description 2
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- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 239000000796 flavoring agent Substances 0.000 description 2
- 235000019634 flavors Nutrition 0.000 description 2
- 230000037406 food intake Effects 0.000 description 2
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 2
- 108010050792 glutenin Proteins 0.000 description 2
- 239000000543 intermediate Substances 0.000 description 2
- 230000000873 masking effect Effects 0.000 description 2
- KIDHWZJUCRJVML-UHFFFAOYSA-N putrescine Chemical compound NCCCCN KIDHWZJUCRJVML-UHFFFAOYSA-N 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- ATHGHQPFGPMSJY-UHFFFAOYSA-N spermidine Chemical compound NCCCCNCCCN ATHGHQPFGPMSJY-UHFFFAOYSA-N 0.000 description 2
- PFNFFQXMRSDOHW-UHFFFAOYSA-N spermine Chemical compound NCCCNCCCCNCCCN PFNFFQXMRSDOHW-UHFFFAOYSA-N 0.000 description 2
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- GNFTZDOKVXKIBK-UHFFFAOYSA-N 3-(2-methoxyethoxy)benzohydrazide Chemical compound COCCOC1=CC=CC(C(=O)NN)=C1 GNFTZDOKVXKIBK-UHFFFAOYSA-N 0.000 description 1
- FGUUSXIOTUKUDN-IBGZPJMESA-N C1(=CC=CC=C1)N1C2=C(NC([C@H](C1)NC=1OC(=NN=1)C1=CC=CC=C1)=O)C=CC=C2 Chemical compound C1(=CC=CC=C1)N1C2=C(NC([C@H](C1)NC=1OC(=NN=1)C1=CC=CC=C1)=O)C=CC=C2 FGUUSXIOTUKUDN-IBGZPJMESA-N 0.000 description 1
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- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- YTAHJIFKAKIKAV-XNMGPUDCSA-N [(1R)-3-morpholin-4-yl-1-phenylpropyl] N-[(3S)-2-oxo-5-phenyl-1,3-dihydro-1,4-benzodiazepin-3-yl]carbamate Chemical compound O=C1[C@H](N=C(C2=C(N1)C=CC=C2)C1=CC=CC=C1)NC(O[C@H](CCN1CCOCC1)C1=CC=CC=C1)=O YTAHJIFKAKIKAV-XNMGPUDCSA-N 0.000 description 1
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- 239000003054 catalyst Substances 0.000 description 1
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- 235000004554 glutamine Nutrition 0.000 description 1
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- 230000001404 mediated effect Effects 0.000 description 1
- KPNBUPJZFJCCIQ-LURJTMIESA-N methyl L-lysinate Chemical compound COC(=O)[C@@H](N)CCCCN KPNBUPJZFJCCIQ-LURJTMIESA-N 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
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- 235000019629 palatability Nutrition 0.000 description 1
- 235000015927 pasta Nutrition 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
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- 150000003138 primary alcohols Chemical class 0.000 description 1
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- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A21—BAKING; EDIBLE DOUGHS
- A21D—TREATMENT OF FLOUR OR DOUGH FOR BAKING, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS
- A21D8/00—Methods for preparing or baking dough
- A21D8/02—Methods for preparing dough; Treating dough prior to baking
- A21D8/04—Methods for preparing dough; Treating dough prior to baking treating dough with microorganisms or enzymes
- A21D8/042—Methods for preparing dough; Treating dough prior to baking treating dough with microorganisms or enzymes with enzymes
-
- A—HUMAN NECESSITIES
- A21—BAKING; EDIBLE DOUGHS
- A21D—TREATMENT OF FLOUR OR DOUGH FOR BAKING, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS
- A21D13/00—Finished or partly finished bakery products
- A21D13/06—Products with modified nutritive value, e.g. with modified starch content
- A21D13/064—Products with modified nutritive value, e.g. with modified starch content with modified protein content
- A21D13/066—Gluten-free products
-
- A—HUMAN NECESSITIES
- A21—BAKING; EDIBLE DOUGHS
- A21D—TREATMENT OF FLOUR OR DOUGH FOR BAKING, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS
- A21D2/00—Treatment of flour or dough by adding materials thereto before or during baking
- A21D2/08—Treatment of flour or dough by adding materials thereto before or during baking by adding organic substances
- A21D2/24—Organic nitrogen compounds
- A21D2/26—Proteins
- A21D2/267—Microbial proteins
-
- A—HUMAN NECESSITIES
- A21—BAKING; EDIBLE DOUGHS
- A21D—TREATMENT OF FLOUR OR DOUGH FOR BAKING, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS
- A21D2/00—Treatment of flour or dough by adding materials thereto before or during baking
- A21D2/08—Treatment of flour or dough by adding materials thereto before or during baking by adding organic substances
- A21D2/24—Organic nitrogen compounds
- A21D2/26—Proteins
- A21D2/268—Hydrolysates from proteins
Definitions
- the present invention is generally applicable to the field of food treatment and
- TG-ase trans-glutaminase
- gluten-free have a mediocre appearance and a poor palatability, with a resulting impaired life quality for people suffering from celiac disease.
- deglutinated flours starting from genetically modified organisms to delete the gene pool responsible for the synthesis of gliadin and glutenin (major components of gluten), is extremely expensive and laborious.
- trans-glutaminase is also known in the food industry, in combination with regular gluten flours, with the ultimate purpose of improving the rheology and technological properties of dough, to perform enrichment in protein content and possibly an overall organoleptic improvement.
- a method for the treatment of celiac disease which involves the use of lysine, a derivative thereof or other simple amines such as methylamine, ethylamine, putrescine, spermidine and spermine as TG-ase co-substrates, for the molecular sequestration of specific portions of the gliadin and possibly for the glutenin, for the deamidation of a glutamine residue in specific sequences of the gluten, since this document argues, although it is not uniquely determined, that just a deamidation of specific glutamines would exclusively trigger the immune response of celiac patients.
- the described process is implemented by acting directly on flour and not on intermediates of the production, i.e. on the dough, with resulting effects in terms of higher costs for the final product.
- WO2008053310 describes a method of treatment of flour-based food and their use by celiac subjects, which involves the use of TG-ase as a gluten masking catalyst, also in this case by acting directly on flour but through transamidation.
- the substrate masking gluten is a derivative of lysine, precisely an ester of this aminoacid with a primary alcohol in one, two, three or four carbon atoms or, possibly, a lysine peptide derivative or another primary amine and therefore always through relatively complex chemical treatments, highlighting as a result the aforementioned technological problems and costs.
- the process focuses on flour and not directly on the semi-finished intermediate.
- the object of the invention is to overcome the above drawbacks, providing a process for the preparation of semi-finished flour-based food which is particularly efficient and relatively cheap.
- a particular object is to provide a process for the preparation of semi-finished flour- based foods which allows to obtain products with a low content of gluten or labelled gluten-free, using any vegetable flour containing gluten and avoiding the use of flours bio-engineered for not expressing the gluten.
- a particular object is to provide a process for the preparation of semi-finished flour- based foods which allows to obtain products with a low content of gluten or labelled gluten-free, by acting directly in the mixing phase of the raw materials and without the use of special flours.
- a further object is to provide a process for the preparation of semi-finished flour-based foods which allows to obtain products with a low content of gluten or classifiable as gluten-free, using natural components already employed in oven -baked goods.
- Still another particular object is to provide a process for the preparation of semi-finished flour-based foods which allows to obtain products with a low content of gluten or classifiable as gluten-free intended to cancel either the causes that generate the celiac disease and the risk associated with gluten ingestion.
- Another particular object is to provide a process for the preparation of semi-finished flour-based foods which allows to obtain products with a low content of gluten or labelled gluten-free which allow to have products matching to traditional products both for organoleptic and rheological properties and with regard to flavour and taste.
- Not last object of the invention is to provide a process for the preparation of semifinished flour-based foods which allows to obtain products with a low content of gluten or labelled gluten-free, and which can be implemented in traditional industrial systems, without making substantial modifications thereto, but only with the insertion of simple to build and easy-to-use auxiliary equipments.
- a process for the preparation of semi-finished flour-based food which, in accordance with claim 1, comprises the steps of providing a predetermined amount of at least one vegetable flour containing gluten, realizing a semi-finished dough product based on said at least one vegetable flour, adding to said dough an element with transglutaminase activity, adding at least one source of lysine adapted to cooperate with the element with trans-glutaminase activity to activate its chelating action of the gluten QXP antigenic sites by trans-amidation, wherein said lysine source is a biological or cellular lysate obtained by mechanical or physical treatments of natural products and added directly into said semi-finished dough.
- the flour gluten network will not be altered, then the dough obtained from working said semi-finished product will show optimal elasticity and strength, suitable to allow the processing of semi-finished product in traditional plants.
- said lysate may be used in raw form or as a supernatant and derived from the treatment of a microorganism containing lysine, such as a microorganism selected from Saccharomyces spp.; Schizosaccharomyces spp.; Saccharomycopsis spp.; Lactobacillus spp.; Leuconostoc spp.; Pediococcus spp.; Bifidobacterium spp.; Ruminococcus spp.; Selenomonas spp.; Glucobacter spp.; Chlamydomonas spp.; Chlorella spp.; Chlorobium spp.; Chlorococcum spp.; Spirulina spp.; Volvox spp.; Spyrogyra spp.; Cytophaga spp.; Rhodobacter spp.; Rhodopse
- the microorganisms or other lysine sources may be subjected to a cold sonication or other mechanical treatments, such as homogenization or centrifugation, that do not require any modification of plants but the addition of simple and easy-to-use auxiliary equipments, in such a manner to not significantly increase the overall costs.
- mechanical treatments such as homogenization or centrifugation will allow to at least partially provide the element with trans-glutaminase activity, also avoiding the use of further bacterial TG-ase in the mixing phase.
- FIG. 1 is a block diagram of a first preferred embodiment of the process
- FIG. 2 is a block diagram of a second preferred form of execution of the process.
- a first mode of carrying out the invention is showed, which essentially comprises a step a) of providing a predetermined amount of a vegetable flour containing gluten or a mixture of vegetable flours, at least one of which contains gluten, in variable proportions and amounts depending on the recipe.
- step ao Further ingredients are subsequently added (step ao) to flour or flour mixture, and in particular one or more liquid phases, in order to achieve a semi-finished dough (step b). Also in this case, of course, the choice of the other components may be highly dependent on the desired finished product.
- the mixture will then be added (step c) with a trans-glutaminase activity element, which could be directly added to the mixture or introduced together with the other ingredients.
- the trans-glutaminase element may be of bacterial origin.
- the dough is then added (step d) with at least one source of lysine adapted to cooperate with the element with TG-ase activity to activate its chelating action on the gluten QXP antigenic sites by trans-amidation, thus obtaining a food product suitable for subjects with celiac disease or other gluten-related disease.
- the source of lysine, or one or more of the provided lysine sources, will be a biological or cellular lysate obtained by mechanical or physical treatments of natural products and added directly into the semi-finished dough.
- the lysate may be used in raw form or as a supernatant resulting from treatment of a microorganism containing lysine, such as yeasts or chlorophyceae (green microalgae), with selection of strains considered non-pathogenic to man.
- a microorganism containing lysine such as yeasts or chlorophyceae (green microalgae)
- the microorganism will be selected among the non-pathogenic strains of Saccharomyces spp., Schizosaccharomyces spp., Saccharomycopsis spp., Lactobacillus spp., Leuconostoc spp., Pediococcus spp., Bifidobacterium spp., Ruminococcus spp., Selenomonas spp., Glucobacter spp., Chlamydomonas spp., Chlorella spp., Chlorobium spp., Chlorococcum spp., Spirulina spp., Volvox spp., Spyrogyra spp., Cytophaga spp., Pvhodobacter spp., Rhodopseudomonas spp., Rhodo spirillum spp., Rhodomicrobium
- Desulfovibrium spp. Flavobacterium spp., Desulfuromonas spp., Thiobacillus spp., Paracoccus spp., Sorangium spp., Rhizobium spp., Agrobacterium spp.
- the lysine source or one of the sources of lysine may be milk, in any form, added directly to the dough.
- the lysine source or one of the sources of lysine may be selected among elements containing and/or producing nisin, such as non-pathogenic strains of Streptococcus spp., Staphylococcus spp., Ruminococcus spp., Bacillus spp., Carnobacterium spp., Halobacterium spp., Actinoplanes spp., Kluyveromyces spp., Leuconostoc spp. and Lactobacillus spp.
- nisin such as non-pathogenic strains of Streptococcus spp., Staphylococcus spp., Ruminococcus spp., Bacillus spp., Carnobacterium spp., Halobacterium spp., Actinoplanes spp., Kluyveromyces spp., Leuconostoc spp. and Lactobacillus
- step eo the suitably prepared micro-organism (step eo) is subjected to cold sonication treatment (step e), adapted to achieve the lysis of the fungal cell wall for generating a cell lysate which make available the lysine necessary for the TG-ase to mask the gluten QXP antigenic sites.
- the lysate is obtained by the action of ultrasounds on regular baker's yeast, that can be immersed in a basin of cold water, which acts as a cooling medium, and treated for 2.5 minutes with ultrasonic frequencies.
- step e) of sonication is followed by a step f) of centrifugation necessary to separate (step g) the supernatant from the solid sediment, that can be separately collected (step h) and possibly removed (step i), while the supernatant will be introduced in the dough (step d).
- the complex of the steps of mechanical treatment of the selected microorganism may be performed in parallel to the step of preparation of the dough, or before the same. In the latter case it will be appropriate to provide a cooling phase of the lysate below 0°C, preferably close to -20°C, to prevent hydrolysis reactions and the lysate will be maintained cooled until its addition in the semi-finished product or dough.
- dough itself Before adding the dough with a lysine source, dough itself can be added (step j) with further adjuvants like a source of papain, purified and crystallized as a single enzyme or as a recombinant enzyme, to take advantage of its transamidase ability by pH variation of the dough in the range of values between 5.7 and 7.5 and in particular of its ability to hydrolyze the proteins in the supernatant derived from the mechanical treatment, to enhance the reaction with transglutaminase contained in the solid sediment.
- further adjuvants like a source of papain, purified and crystallized as a single enzyme or as a recombinant enzyme, to take advantage of its transamidase ability by pH variation of the dough in the range of values between 5.7 and 7.5 and in particular of its ability to hydrolyze the proteins in the supernatant derived from the mechanical treatment, to enhance the reaction with transglutaminase contained in the solid sediment.
- a further additive may be made up from at least one source of the enzyme 1,3-beta- glucanase, and the Class II and III chitinases, for example fresh papaya juice or any papaya-based sample or compound, in order to release the PNG-ase within the microorganism cell wall fraction, through degradation of the cell wall polysaccharides themselves exerted by these enzymes.
- the enzyme 1,3-beta- glucanase for example fresh papaya juice or any papaya-based sample or compound
- Additional additives to the lysate may be non-toxic reducing agents selected from the group comprising sorbic acid, benzoic acid, sodium metabisulfite, potassium metabisulfite, calcium metabisulfite, ascorbic acid, citric acid, tartaric acid, L-cysteine, L-cysteine hydrochloride, L-cysteine hydrochloride monohydrate, and similar agents to reactivate the cell wall PNG-ase of the microorganism.
- non-toxic reducing agents selected from the group comprising sorbic acid, benzoic acid, sodium metabisulfite, potassium metabisulfite, calcium metabisulfite, ascorbic acid, citric acid, tartaric acid, L-cysteine, L-cysteine hydrochloride, L-cysteine hydrochloride monohydrate, and similar agents to reactivate the cell wall PNG-ase of the microorganism.
- the dough so obtained will undergo one or more subsequent accessory steps, such as a resting step k) for a predetermined time, e.g. 60 minutes, a step 1) of new kneading with the possible addition of yeast (phase lo), a possible step m) of leavening in the case where the semi-finished product is intended for the production of bakery products, a portioning step n), and further steps o) of cooking or other storage procedure designed to obtain the product P ready for consumption and/or sale.
- a resting step k for a predetermined time, e.g. 60 minutes
- a possible step m) of leavening in the case where the semi-finished product is intended for the production of bakery products
- a portioning step n a portioning step n
- Fig. 2 shows a second mode of carrying out the process, which differs from the previous essentially because the step e) of the lysine source sonication is replaced by a mechanical treatment of centrifugation, for example using a piston-rod mechanical homogenizer, in order to release either the lysine useful to the enzymatic reaction and the cell wall with PNG-ase activity, to replace the external supplementation of bacterial TG-ase or as partial addition to the external Tg-ase amount itself.
- a mechanical treatment of centrifugation for example using a piston-rod mechanical homogenizer
- Treating the supernatant with papain will hydrolyze its protein content, making more easily available for the reaction with TG-ase contained in the sediment, which therefore will also be suitably introduced into the dough.
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- Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- General Health & Medical Sciences (AREA)
- Nutrition Science (AREA)
- Microbiology (AREA)
- Bakery Products And Manufacturing Methods Therefor (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Cereal-Derived Products (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| IT000002A ITSR20130002A1 (it) | 2013-10-08 | 2013-10-08 | Nuovo processo industriale di lavorazione per la produzione di alimenti farinacei, destinati a soggetti con malattia celiaca clinicamente manifesta, a base di farine comuni. |
| PCT/IB2014/065152 WO2015052665A1 (en) | 2013-10-08 | 2014-10-08 | Process for the preparation of semi-finished flour based food products comprising an element with trans-glutaminas activity and a source of lysine |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| EP3071041A1 true EP3071041A1 (de) | 2016-09-28 |
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| Application Number | Title | Priority Date | Filing Date |
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| EP14798966.9A Withdrawn EP3071041A1 (de) | 2013-10-08 | 2014-10-08 | Verfahren zur herstellung halbfertiger nahrungsmittelprodukte auf mehlbasis mit trans-glutaminase-aktivität und einer lysinquelle |
Country Status (3)
| Country | Link |
|---|---|
| EP (1) | EP3071041A1 (de) |
| IT (1) | ITSR20130002A1 (de) |
| WO (1) | WO2015052665A1 (de) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
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| CN107751307A (zh) * | 2017-12-06 | 2018-03-06 | 王康学 | 一种螺旋藻月饼及其制备方法 |
| IT201800010305A1 (it) * | 2018-11-13 | 2020-05-13 | Danilo Ciciulla | Procedimento per la preparazione di alimenti a base di farina di grano destinati a soggetti celiaci o affetti da gluten sensitivity |
| BR112022025272A2 (pt) * | 2020-06-09 | 2023-02-14 | Dr Schaer S P A | Método para preparar uma mistura e produtos alimentares derivados do mesmo |
| ES2970628A1 (es) * | 2022-10-25 | 2024-05-29 | Bread Free S L | Procedimiento para preparar una harina apta para celíacos |
Family Cites Families (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR947040A (fr) * | 1947-05-13 | 1949-06-21 | Extrait concentré vitaminé et biscuit contenant cet extrait | |
| US3650764A (en) * | 1970-03-30 | 1972-03-21 | H C Brill Co Inc | Enzymatic baking compositions and methods for using same |
| CH643296A5 (fr) * | 1980-05-02 | 1984-05-30 | Nestle Sa | Procede de fabrication d'un extrait de levure. |
| US4904485A (en) * | 1986-10-02 | 1990-02-27 | Kanegafuchi Kagaku Kogyo Kabushiki Kaisha | Fat compositions suitable for use in bakeries or confectioneries |
| DE4041533A1 (de) * | 1990-12-22 | 1992-06-25 | Roehm Gmbh | Backmittel oder backmehl, sowie verfahren zur herstellung von backteigen und backwaren |
| JPH11243843A (ja) * | 1998-02-27 | 1999-09-14 | Ajinomoto Co Inc | パン類の製造方法及びパン類製造用酵素製剤 |
| JP3867261B2 (ja) * | 1998-04-08 | 2007-01-10 | 味の素株式会社 | 酵素製剤及び麺類の製造方法 |
| EP1075267A2 (de) * | 1998-05-06 | 2001-02-14 | Kobenhavns Universitet | Behandlung der zöliakie (einheimische sprue) |
| AU761467B2 (en) * | 1998-06-09 | 2003-06-05 | Ajinomoto Co., Inc. | Novel enzyme-treated protein-containing food, and methods for producing the same |
| DE10046605A1 (de) * | 2000-09-20 | 2002-03-28 | Roehm Enzyme Gmbh | Verwendung von Transglutaminasen zur Herstellung von weizenarmen Backwaren |
| ITMI20062080A1 (it) * | 2006-10-30 | 2008-04-30 | Consiglio Nazionale Ricerche | Trattamento di farine di cereali per il consumo alimentare da parte di pazienti celiaci |
| WO2010015554A1 (en) * | 2008-08-05 | 2010-02-11 | Dsm Ip Assets B.V. | Novel starch composition and method to produce a baked product |
| US20100316764A1 (en) * | 2009-06-10 | 2010-12-16 | Engrain, LLC | Flour supplement compositions and methods for preparing wheat flour |
| WO2011130576A1 (en) * | 2010-04-14 | 2011-10-20 | Solazyme, Inc. | Oleaginous yeast food compositions |
| FR2973989A1 (fr) * | 2011-04-15 | 2012-10-19 | Nutrionix | Nouvel agent substitut du sel nacl, son utilisation et produits en contenant |
| PL223886B1 (pl) * | 2011-07-20 | 2016-10-31 | Pmt Trading Spółka Z Ograniczoną Odpowiedzialnością | Sposób produkcji pieczywa na zakwasie |
-
2013
- 2013-10-08 IT IT000002A patent/ITSR20130002A1/it unknown
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2014
- 2014-10-08 EP EP14798966.9A patent/EP3071041A1/de not_active Withdrawn
- 2014-10-08 WO PCT/IB2014/065152 patent/WO2015052665A1/en not_active Ceased
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| Title |
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| None * |
| See also references of WO2015052665A1 * |
Also Published As
| Publication number | Publication date |
|---|---|
| WO2015052665A4 (en) | 2015-06-04 |
| WO2015052665A1 (en) | 2015-04-16 |
| ITSR20130002A1 (it) | 2015-04-08 |
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