EP1802204A1 - Protection d'ingrédients alimentaires bioactifs par l'utilisation d'ingrédients leurres - Google Patents
Protection d'ingrédients alimentaires bioactifs par l'utilisation d'ingrédients leurresInfo
- Publication number
- EP1802204A1 EP1802204A1 EP05794531A EP05794531A EP1802204A1 EP 1802204 A1 EP1802204 A1 EP 1802204A1 EP 05794531 A EP05794531 A EP 05794531A EP 05794531 A EP05794531 A EP 05794531A EP 1802204 A1 EP1802204 A1 EP 1802204A1
- Authority
- EP
- European Patent Office
- Prior art keywords
- food
- bioactive
- food product
- ingredient
- interest
- 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- Withdrawn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
- 230000000975 bioactive effect Effects 0.000 title claims abstract description 97
- 235000012041 food component Nutrition 0.000 title claims abstract description 83
- 239000005417 food ingredient Substances 0.000 title claims abstract description 83
- 239000004615 ingredient Substances 0.000 title claims abstract description 58
- 238000000034 method Methods 0.000 title claims description 15
- 235000013305 food Nutrition 0.000 claims abstract description 75
- 244000005700 microbiome Species 0.000 claims abstract description 56
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 119
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 48
- 239000000047 product Substances 0.000 claims description 46
- 238000000855 fermentation Methods 0.000 claims description 36
- 230000004151 fermentation Effects 0.000 claims description 36
- LWGJTAZLEJHCPA-UHFFFAOYSA-N n-(2-chloroethyl)-n-nitrosomorpholine-4-carboxamide Chemical compound ClCCN(N=O)C(=O)N1CCOCC1 LWGJTAZLEJHCPA-UHFFFAOYSA-N 0.000 claims description 26
- 241000194020 Streptococcus thermophilus Species 0.000 claims description 24
- 239000000203 mixture Substances 0.000 claims description 24
- 235000018102 proteins Nutrition 0.000 claims description 24
- 102000004169 proteins and genes Human genes 0.000 claims description 24
- 108090000623 proteins and genes Proteins 0.000 claims description 24
- 241000894006 Bacteria Species 0.000 claims description 23
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 claims description 22
- 235000013365 dairy product Nutrition 0.000 claims description 15
- 230000004060 metabolic process Effects 0.000 claims description 14
- 238000002360 preparation method Methods 0.000 claims description 14
- 239000012634 fragment Substances 0.000 claims description 13
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 claims description 11
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 claims description 11
- 235000014655 lactic acid Nutrition 0.000 claims description 11
- 239000004310 lactic acid Substances 0.000 claims description 11
- 108010076119 Caseins Proteins 0.000 claims description 10
- 235000021240 caseins Nutrition 0.000 claims description 10
- 230000008569 process Effects 0.000 claims description 10
- 238000004519 manufacturing process Methods 0.000 claims description 8
- 230000015572 biosynthetic process Effects 0.000 claims description 7
- 239000005018 casein Substances 0.000 claims description 7
- 238000003786 synthesis reaction Methods 0.000 claims description 7
- 108010067454 caseinomacropeptide Proteins 0.000 claims description 6
- 235000013376 functional food Nutrition 0.000 claims description 6
- 238000011065 in-situ storage Methods 0.000 claims description 6
- 229910052757 nitrogen Inorganic materials 0.000 claims description 6
- 241000186660 Lactobacillus Species 0.000 claims description 5
- 235000015097 nutrients Nutrition 0.000 claims description 5
- 229940039696 lactobacillus Drugs 0.000 claims description 4
- 235000013311 vegetables Nutrition 0.000 claims description 4
- 108010006701 N-acetyllysyl-arginyl-tyrosyl-asparaginyl-leucinamide Proteins 0.000 claims description 3
- AOKLUWFWNZLQSN-LROMGURASA-N (2s)-2-[[(2s)-2-[[(2s)-2-[[(2s)-2-acetamido-6-aminohexanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-n-[(2s)-1-amino-4-methyl-1-oxopentan-2-yl]butanediamide Chemical compound NCCCC[C@H](NC(C)=O)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(N)=O)CC1=CC=C(O)C=C1 AOKLUWFWNZLQSN-LROMGURASA-N 0.000 claims description 2
- 241000186000 Bifidobacterium Species 0.000 claims description 2
- 241000194036 Lactococcus Species 0.000 claims description 2
- 241000194017 Streptococcus Species 0.000 claims description 2
- VNYDHJARLHNEGA-RYUDHWBXSA-N Tyr-Pro Chemical compound C([C@H](N)C(=O)N1[C@@H](CCC1)C(O)=O)C1=CC=C(O)C=C1 VNYDHJARLHNEGA-RYUDHWBXSA-N 0.000 claims description 2
- 235000014121 butter Nutrition 0.000 claims description 2
- 108010020532 tyrosyl-proline Proteins 0.000 claims description 2
- FQYQMFCIJNWDQZ-CYDGBPFRSA-N Ile-Pro-Pro Chemical compound CC[C@H](C)[C@H](N)C(=O)N1CCC[C@H]1C(=O)N1[C@H](C(O)=O)CCC1 FQYQMFCIJNWDQZ-CYDGBPFRSA-N 0.000 claims 1
- 239000012467 final product Substances 0.000 claims 1
- 108010031424 isoleucyl-prolyl-proline Proteins 0.000 claims 1
- 108010015385 valyl-prolyl-proline Proteins 0.000 claims 1
- SKGURMFKEAFAGD-CSYZDTNESA-N C([C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O)C1=CC=C(O)C=C1 Chemical compound C([C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O)C1=CC=C(O)C=C1 SKGURMFKEAFAGD-CSYZDTNESA-N 0.000 description 18
- 235000013336 milk Nutrition 0.000 description 16
- 239000008267 milk Substances 0.000 description 16
- 210000004080 milk Anatomy 0.000 description 16
- 108010046377 Whey Proteins Proteins 0.000 description 12
- 239000003531 protein hydrolysate Substances 0.000 description 12
- 150000001875 compounds Chemical class 0.000 description 11
- 235000021119 whey protein Nutrition 0.000 description 11
- 102000011632 Caseins Human genes 0.000 description 9
- 230000000694 effects Effects 0.000 description 8
- 238000003860 storage Methods 0.000 description 8
- 235000013618 yogurt Nutrition 0.000 description 6
- 108090000790 Enzymes Proteins 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 5
- 230000008901 benefit Effects 0.000 description 5
- 238000010438 heat treatment Methods 0.000 description 5
- 150000002500 ions Chemical class 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- 102000007544 Whey Proteins Human genes 0.000 description 4
- 150000001413 amino acids Chemical class 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 235000014048 cultured milk product Nutrition 0.000 description 4
- 230000002255 enzymatic effect Effects 0.000 description 4
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 102000014171 Milk Proteins Human genes 0.000 description 3
- 108010011756 Milk Proteins Proteins 0.000 description 3
- 229940021722 caseins Drugs 0.000 description 3
- 230000015556 catabolic process Effects 0.000 description 3
- 235000015140 cultured milk Nutrition 0.000 description 3
- 238000006731 degradation reaction Methods 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 235000011389 fruit/vegetable juice Nutrition 0.000 description 3
- 230000007407 health benefit Effects 0.000 description 3
- 238000004128 high performance liquid chromatography Methods 0.000 description 3
- 230000007062 hydrolysis Effects 0.000 description 3
- 238000006460 hydrolysis reaction Methods 0.000 description 3
- 238000004895 liquid chromatography mass spectrometry Methods 0.000 description 3
- 230000002503 metabolic effect Effects 0.000 description 3
- 235000021239 milk protein Nutrition 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 230000001681 protective effect Effects 0.000 description 3
- 238000011002 quantification Methods 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 2
- 102100038920 Alpha-S1-casein Human genes 0.000 description 2
- 102000004506 Blood Proteins Human genes 0.000 description 2
- 108010017384 Blood Proteins Proteins 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 108010009736 Protein Hydrolysates Proteins 0.000 description 2
- 229920002472 Starch Polymers 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- 230000000845 anti-microbial effect Effects 0.000 description 2
- 229920001525 carrageenan Polymers 0.000 description 2
- 235000010418 carrageenan Nutrition 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 235000020247 cow milk Nutrition 0.000 description 2
- 230000008034 disappearance Effects 0.000 description 2
- 235000019253 formic acid Nutrition 0.000 description 2
- 238000013467 fragmentation Methods 0.000 description 2
- 238000006062 fragmentation reaction Methods 0.000 description 2
- 235000015203 fruit juice Nutrition 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 235000020256 human milk Nutrition 0.000 description 2
- 210000004251 human milk Anatomy 0.000 description 2
- 230000003834 intracellular effect Effects 0.000 description 2
- 238000004811 liquid chromatography Methods 0.000 description 2
- 239000001814 pectin Substances 0.000 description 2
- 229920001277 pectin Polymers 0.000 description 2
- 235000010987 pectin Nutrition 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 239000003381 stabilizer Substances 0.000 description 2
- 235000019698 starch Nutrition 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 235000000346 sugar Nutrition 0.000 description 2
- 235000020357 syrup Nutrition 0.000 description 2
- 239000006188 syrup Substances 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 239000003643 water by type Substances 0.000 description 2
- 108050000244 Alpha-s1 casein Proteins 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 102000005593 Endopeptidases Human genes 0.000 description 1
- 108010059378 Endopeptidases Proteins 0.000 description 1
- 102000018389 Exopeptidases Human genes 0.000 description 1
- 108010091443 Exopeptidases Proteins 0.000 description 1
- BDAGIHXWWSANSR-UHFFFAOYSA-M Formate Chemical compound [O-]C=O BDAGIHXWWSANSR-UHFFFAOYSA-M 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000741048 Homo sapiens Alpha-S1-casein Proteins 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical class [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- 206010020772 Hypertension Diseases 0.000 description 1
- 241000186673 Lactobacillus delbrueckii Species 0.000 description 1
- 102000003939 Membrane transport proteins Human genes 0.000 description 1
- 108090000301 Membrane transport proteins Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 240000007594 Oryza sativa Species 0.000 description 1
- 235000007164 Oryza sativa Nutrition 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 108010064851 Plant Proteins Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108010073771 Soybean Proteins Proteins 0.000 description 1
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
- GIAZPLMMQOERPN-YUMQZZPRSA-N Val-Pro Chemical compound CC(C)[C@H](N)C(=O)N1CCC[C@H]1C(O)=O GIAZPLMMQOERPN-YUMQZZPRSA-N 0.000 description 1
- 239000005862 Whey Substances 0.000 description 1
- PQLVXDKIJBQVDF-UHFFFAOYSA-N acetic acid;hydrate Chemical compound O.CC(O)=O PQLVXDKIJBQVDF-UHFFFAOYSA-N 0.000 description 1
- 230000000202 analgesic effect Effects 0.000 description 1
- 235000021120 animal protein Nutrition 0.000 description 1
- 230000001093 anti-cancer Effects 0.000 description 1
- 230000003276 anti-hypertensive effect Effects 0.000 description 1
- 230000002180 anti-stress Effects 0.000 description 1
- 230000002785 anti-thrombosis Effects 0.000 description 1
- 239000003146 anticoagulant agent Substances 0.000 description 1
- 229940030600 antihypertensive agent Drugs 0.000 description 1
- 239000002220 antihypertensive agent Substances 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 125000004429 atom Chemical group 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 235000013361 beverage Nutrition 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000037180 bone health Effects 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 229960005069 calcium Drugs 0.000 description 1
- 125000004432 carbon atom Chemical group C* 0.000 description 1
- 210000000748 cardiovascular system Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 235000013351 cheese Nutrition 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- 230000007123 defense Effects 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 210000002249 digestive system Anatomy 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 108010020477 exorphins Proteins 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 235000021107 fermented food Nutrition 0.000 description 1
- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- 238000000227 grinding Methods 0.000 description 1
- 229910052736 halogen Inorganic materials 0.000 description 1
- 150000002367 halogens Chemical class 0.000 description 1
- 125000005842 heteroatom Chemical group 0.000 description 1
- 230000036571 hydration Effects 0.000 description 1
- 238000006703 hydration reaction Methods 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 239000000413 hydrolysate Substances 0.000 description 1
- 235000015243 ice cream Nutrition 0.000 description 1
- 230000002519 immonomodulatory effect Effects 0.000 description 1
- 230000003308 immunostimulating effect Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 239000000543 intermediate Substances 0.000 description 1
- 238000005040 ion trap Methods 0.000 description 1
- 239000002075 main ingredient Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 210000000653 nervous system Anatomy 0.000 description 1
- QJGQUHMNIGDVPM-UHFFFAOYSA-N nitrogen group Chemical group [N] QJGQUHMNIGDVPM-UHFFFAOYSA-N 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 235000006180 nutrition needs Nutrition 0.000 description 1
- 229940127240 opiate Drugs 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 238000009928 pasteurization Methods 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 235000021118 plant-derived protein Nutrition 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 235000020122 reconstituted milk Nutrition 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002040 relaxant effect Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 235000009566 rice Nutrition 0.000 description 1
- 239000000932 sedative agent Substances 0.000 description 1
- 230000001624 sedative effect Effects 0.000 description 1
- 235000020374 simple syrup Nutrition 0.000 description 1
- 235000020183 skimmed milk Nutrition 0.000 description 1
- 229940001941 soy protein Drugs 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 238000004885 tandem mass spectrometry Methods 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 235000015192 vegetable juice Nutrition 0.000 description 1
- 230000036642 wellbeing Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
- C12N1/20—Bacteria; Culture media therefor
- C12N1/205—Bacterial isolates
-
- 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
- A23C9/123—Fermented milk preparations; Treatment using microorganisms or enzymes using only microorganisms of the genus lactobacteriaceae; Yoghurt
-
- 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
- A23C9/13—Fermented milk preparations; Treatment using microorganisms or enzymes using additives
- A23C9/1322—Inorganic compounds; Minerals, including organic salts thereof, oligo-elements; Amino-acids, peptides, protein-hydrolysates or derivatives; Nucleic acids or derivatives; Yeast extract or autolysate; Vitamins; Antibiotics; Bacteriocins
-
- 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
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2400/00—Lactic or propionic acid bacteria
- A23V2400/11—Lactobacillus
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2400/00—Lactic or propionic acid bacteria
- A23V2400/21—Streptococcus, lactococcus
- A23V2400/249—Thermophilus
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12R—INDEXING SCHEME ASSOCIATED WITH SUBCLASSES C12C - C12Q, RELATING TO MICROORGANISMS
- C12R2001/00—Microorganisms ; Processes using microorganisms
- C12R2001/01—Bacteria or Actinomycetales ; using bacteria or Actinomycetales
- C12R2001/46—Streptococcus ; Enterococcus; Lactococcus
Definitions
- the present invention relates to a food product containing one or more live microorganisms and at least one bioactive food ingredient of interest, wherein the living microorganism (s) and the bioactive food ingredient (s) of interest are used in such a way as to reduce the metabolisation of said bioactive ingredient (s) by said microorganism (s).
- Bioactive peptides are defined sequences of amino acids that are inactive in their original protein, but which have particular properties once released by enzymatic action. They are also called functional peptides. These bioactive peptides are capable of exerting, inter alia, an effect on the digestive system, the defenses of the body (for example, an antimicrobial or immunomodulatory effect), the cardiovascular system (in particular an antithrombotic or antihypertensive effect), and or the nervous system (such as a sedative and analgesic effect of the opioid type) (see Tables 1 and 2 below). Table 1 below lists the main functional peptides released by the hydrolysis of the proteins of human milk and cow's milk.
- Table 2 below lists the main physiological activities of functional peptides from milk known to date.
- peptides are most often obtained by hydrolysis of plant proteins (for example soy proteins) or animal proteins (for example, caseins or serum proteins of milk), hydrolysis generated by enzymatic and / or fermentative processes, most often accompanied by a concentration of the active fraction, a step usually necessary to provide the targeted "health benefit".
- plant proteins for example soy proteins
- animal proteins for example, caseins or serum proteins of milk
- hydrolysis generated by enzymatic and / or fermentative processes most often accompanied by a concentration of the active fraction, a step usually necessary to provide the targeted "health benefit”.
- the manufacture and use of these peptides for a health benefit is the subject of an abundant literature (see the Danone World Newsletter N ° 17 of September 1998).
- fermented milk products are in a good position because of their health benefits due to the presence of ferments and fermentation products (ie the molecules resulting from the transformation , by lactic acid bacteria, substrates present in the milk).
- PRT wall proteases which cuts proteins and large peptides to facilitate their assimilation ("extracellular metabolism system")
- intracellular enzymatic system capable of degrading the peptides into amino acids (comprising about fifteen endo- and exopeptidases) ("intracellular metabolization system").
- the thermisation of a fermented milk mass involves the use of stabilizers added before the heat treatment (pectins, starches, carrageenans, etc.), which complicates the process and significantly increases the cost of the formula;
- the organoleptic impact generally negative, is significant.
- the Applicant provides a solution that satisfies the existing need.
- the present invention is therefore concerned with a food product containing one or more living microorganisms and at least one bioactive food ingredient of interest, characterized in that the living microorganism (s) and the bioactive food ingredient (s) of interest are placed in in order to reduce the metabolisation of said bioactive ingredient (s) by said living microorganism (s).
- the Applicant has been able to show that one or more bioactive food ingredients of interest could be effectively protected against metabolism by living microorganisms, provided that the conditions for use with each other are appropriate.
- Such appropriate implementation conditions may involve a variety of means, including: (a) the use of live microorganisms with reduced ability to metabolize bioactive ingredients; and / or (b) the use of lure food ingredients that are deliberately “fed” to living microorganisms; and / or c) the implementation of a physical protection of the bioactive ingredients, in particular by encapsulation of the latter.
- An object of the present invention is therefore a food product containing one or more living microorganisms and at least one bioactive food ingredient of interest, characterized in that the one or more bioactive food ingredients of interest are protected:
- the one or more bioactive food ingredients of interest being preferably encapsulated;
- metabolic or “metabolized” is intended to mean, according to the present invention, the transformation or degradation of a substance by one or more living microorganisms, aimed at its consumption as a source of nutrients, and having the final consequence of its disappearance, more or less complete, of the medium.
- the metabolisation of an ingredient is "reduced” if it is less than the metabolism of the same ingredient when the latter ingredient is not protected by at least one of the means provided for in the context of this invention.
- this reduced metabolism tends to, or is worth, zero, which amounts to little, almost no or no metabolism of said ingredient.
- the residual amount of bioactive food ingredient (s) of interest in said food product is, 3 weeks after its preparation, between 50 and 100% approximately relative to the amount of bioactive food ingredient (s) of interest present in the product just after preparation.
- said residual amount is between about 80 and 100%.
- residual amount of bioactive food ingredient (s) of interest in said food product is meant according to the present invention the percentage of bioactive food ingredient (s) d interest present in said food product when the latter is maintained under suitable storage conditions (for example, of the order of 4 to 10 0 C for a fresh product) for 3 weeks, relative to the percentage of ingredient (s) ) bioactive food (s) of interest present at the start, that is to say right after manufacture of the product.
- the food product according to the invention contains at least one decoy food ingredient.
- lure food ingredient is intended to denote according to the present invention a food ingredient (preferably a peptide, a protein, an analogue or a derivative thereof, and combinations thereof) capable of serving as a source of nutrients (especially Nitrogen source) for living microorganisms, and intended to be preferentially metabolized by said microorganisms, so as to divert the latter from the bioactive ingredients of interest that are of course intended to be preserved as a priority.
- the lure ingredient represents a nutrient source for microorganisms, which is sacrificed deliberately to save as much bioactive ingredients of interest as possible.
- the ingredient Food lure acts in this respect as a competitive inhibitor of the transport of bioactive ingredients of interest.
- the presence of decoy ingredients in the food product makes it possible to use any living microorganism suitable for the manufacture of said product, without it being necessary to take account of its capacity. to metabolize the bioactive ingredient (s).
- the food product contains between about 0.001 and 2% by weight of food ingredient (s) lure (s) relative to the total weight of the finished product.
- the food product contains between about 0.001 and 0.2% by weight of food ingredient (s) decoy (s) relative to the total weight of the finished product.
- the rate of metabolization of the food ingredient (s) decoy food (s) in the food product is, three weeks after its preparation, at least equal to that of the bioactive ingredient (s).
- This rate of metabolism of the food ingredient (s) lure (s) is (s) is preferably greater than that of the food ingredient (s) bioactive (s) of interest.
- the one or more bioactive food ingredients of interest and / or the one or more lure food ingredients are chosen from: proteins,
- the bioactive food ingredient of interest is chosen from: ⁇ S1 peptide [91-100] (see European patent EP 0 714910), peptide C6- ⁇ s i 194-199 (see US Pat. No. 6,514 941) , the peptide C7- ⁇ 177-183 (see U.S. Patent No.
- the bioactive food ingredient of interest is selected from: ⁇ S1 peptide [91-100], fragments, analogs, derivatives thereof, proteins and / or peptides containing them, and combinations thereof .
- "Analogous” is understood to mean any modified version of an initial compound, here a protein or a peptide, said modified version possibly being natural or synthetic, in which one or more atoms, such as carbon atoms, d Hydrogen, oxygen, or heteroatoms such as nitrogen, sulfur, or halogen, have been added or removed from the structure of the parent compound to obtain a new molecular compound.
- a “derivative" within the meaning of the invention is any compound that has a resemblance or a structural unit in common with a reference compound (protein or peptide). Also included in this definition are compounds which, alone or with other compounds, may be precursors or intermediates in the synthesis of a reference compound, by means of one or more chemical reactions, and secondly the compounds that can be formed from said reference compound, alone or with other compounds, via one or more chemical reactions.
- hydrolysates in particular tryptic hydrolysates, of proteins and / or peptides, the hydrolyzate fractions, as well as the mixtures of hydrolysates and / or of hydrolysate fractions.
- analogs and derivative of a peptide or protein cover, for example, a glycosylated or phosphorylated peptide or protein or which has undergone any group grafting. chemical.
- the bioactive food ingredient of interest and / or the decoy food ingredient may be sugars or fatty acids.
- the lure food ingredient (s) are nitrogen nutrient sources for the living microorganism (s).
- the one or more lure food ingredients are chosen from:
- the living microorganism (s) have an intact or reduced capacity for metabolizing the one or more bioactive food ingredients of interest.
- a "reduced metabolic capacity" is such that the amount of bioactive ingredients of interest metabolized during fermentation (which therefore disappears from the medium) is less than or equal to 40% of the initial amount of ingredients ( before fermentation). This is mathematically translated as: Qr> 0.6 Q 0 (I) Where:
- the amount of residual bioactive ingredients Q r can be measured by an HPLC liquid chromatography method coupled to an MS / MS type detector.
- An example of an experimental procedure is given in the examples below. It will be preferred to use living microorganisms as bacteria, preferably lactic acid bacteria, as living organisms. More particularly living bacteria will be selected from: o Streptococcus spp, preferably
- Streptococcus thermophilus o Lactobacillus spp. o Lactococcus spp. o Bifidobacterium spp.
- the living bacteria will be chosen from:
- Streptococcus thermophilus deposited at the CNCM on October 24, 1995 under the number 1-1630;
- thermophilus deposited at the CNCM on September 16, 2004 under the number I-3302. More preferably, said living bacteria are S. thermophilus bacteria deposited at the CNCM on 05/01/04 under the number 1-3211.
- the food product contains at least the living bacteria S. thermophilus and Lactobacillus spp.
- said living bacteria Streptococcus thermophilus are chosen from S. thermophilus deposited at the CNCM on 24/01/02 under the number I-2774, S. thermophilus deposited at the CNCM on October 24, 1995 under the number 1-1630, S. thermophilus deposited at the CNCM on May 10, 2004 under the number 1-3211, S. thermophilus deposited at the CNCM on September 16, 2004 under the number 1-3301, and S. thermophilus deposited at the CNCM on March 16 / 09/04 under number I-3302.
- the content of the food product according to the invention in live microorganisms may vary and will be chosen by those skilled in the art in the light of his general knowledge in the field. In practice, a standard overall content, for example of the order of 10 7 to 10 9 bacteria per gram of food product, will preferably be sought.
- the food product according to the present invention is a fermented product. More preferably, the fermented food product is a dairy or vegetable product.
- dairy product in addition to milk, products derived from milk, such as cream, ice cream, butter, cheese, yogurt; secondary products, such as whey, casein; and any prepared food containing, as the main ingredient, milk or milk constituents.
- Plant product means, inter alia, products obtained from a vegetable base such as, for example, fruit juices and vegetable juices, including soya juice, oat juice or the rice juice.
- the above definitions of “dairy product” and “plant product” each cover any product made from a mixture of dairy and vegetable products, such as a mixture of milk and fruit juice, for example.
- the present invention also relates to a method for preparing a food product as defined above, in which one or more decoy food ingredients are added to the mixture intended to constitute said product, preferably after fermentation thereof.
- one or more live microorganisms and one or more bioactive food ingredient (s) of interest and / or one or more food ingredient (s) decoys (s). ) are added one after the other in the mixture intended to constitute said food product.
- the one or more bioactive food ingredients of interest and / or the living microorganism (s) and / or the one or more lure food ingredient (s) are added simultaneously to said mixture.
- the culture conditions of the microorganisms depend on said microorganisms and are known to those skilled in the art.
- the optimum growth temperatures for S. thermophilus are generally between about 36 ° and 42 ° C. they are between 42 ° and 46 ° C for L. delbrueckii spp. bulgaricus (typically found in yoghurt).
- the fermentation stoppage which depends on the desired pH, is obtained by rapid cooling, which slows down the metabolic activity of the microorganisms.
- the one or more bioactive food ingredients of interest and / or the one or more lure food ingredients are prepared directly in the mixture intended to constitute said food product. In this respect, reference will be made to "in situ synthesis" of the bioactive ingredient (s) and / or the lure ingredient (s).
- the present invention further relates to the use of a food product as described above as a functional food.
- a functional food is meant a food product that advantageously affects one or more target functions of the body, regardless of its nutritional effects. This can result in an improvement of the state of health and / or well-being and / or a reduction of the risks of occurrence of diseases in a consumer who ingests normal amounts of said product.
- Examples of activities of a "functional food” include anti-cancer activities, immunostimulatory, promoting bone health, anti-stress, opiates, antihypertensives, calcium bioavailability enhancers, or antimicrobial (Functional Food Science in Europe, 1998). Such functional foods may be intended for humans and / or animals.
- the present invention also relates to the use, in a food product containing one or more living microorganisms and at least one bioactive food ingredient of interest, of at least one food ingredient lure to protect the bioactive food ingredient (s) from interest against metabolism by the living microorganism (s).
- the present invention is illustrated by the following figures, which are in no way limiting.
- FIG. 1 Chromatogram LC-MS illustrating the disappearance of the bioactive peptide ⁇ S1 [91-100] included in the ingredient Lactium® during lactic fermentation.
- Figure 2 Identification and quantification of the main peptides of the Lactium® ingredient by LC-MS / MS before and after fermentation of the dairy "mix” with a ferment consisting of a mixture of strains I-2783 (deposited at the CNCM on 24 / 01/02), I-2774 (filed at the CNCM on 24/01/02), I-2835 (filed at the CNCM on 04/04/02) and 1-1968 (filed at the CNCM on 14/01 / 98). After fermentation, these peptides are only found in trace amounts and merge with the baseline. "? Means that the identification of the sequence was not possible or is not certain; only the mass of the peptide is then reported.
- FIG. 3 Compared peptide profiles (LC-MS / MS chromatograms) of a dairy "mix" containing 1.5 g / L of DMV C 12® hydrolyzate, before (1) and after fermentation (2) up to pH 4.7 by the Hansen YC380 lactic ferment. Almost all the peptides of the hydrolyzate, including the bioactive C12 peptide (fragment ⁇ S1 [23-34]), disappeared following metabolism by the ferment strains.
- FIG. 4 Curves illustrating the evolution of the residual content of bioactive peptide ⁇ S1 [91-100] in a finished product constituted of 95% fermented mass by the ferment containing strains I-2783, I-2774, I-2835 and 1-1968, and 5% aromatised sugar syrup containing ⁇ S1 peptide [91-100], during storage at 10 ° C. The experiment was carried out at the rate of 4 independent tests E1, E2, E3 and E4.
- FIG. 5 Curves illustrating the evolution of the residual content of bioactive peptide ⁇ S1 [91-100], added after fermentation in a fermented product then thermised at 75 ° C. for 1 minute, and stored at 10 ° C. until the date consumption limit (DLC).
- DLC date consumption limit
- Figure 6 Illustration of the evolution of the residual content of bioactive peptide ⁇ S1 [91-100] in a finished product consisting of 95% fermented mass by the ferment containing the strain I-2774 and formate and 5% of syrup flavored sugar containing the peptide ⁇ S1 [91-100] (provided in the form of Lactium®, assayed at 1.5 g / kg of finished product), during storage at 100 ° C. until DLC.
- Figure 7 Graph illustrating the percentage of residual ⁇ S1 [91-100] peptide after fermentation relative to the unfermented control (enzyme containing strains 1-2783, 1-2774, 1-2835 and 1-1968) in the presence of increasing concentrations (0.5, 1.0 and 1.5 g / L) "lure" hydrolysates (Vitalarmor 950, Armor Protein, MPH955, Fonterra).
- FIG. 1 Graph illustrating the percentage of residual ⁇ S1 [91-100] peptide after fermentation relative to the unfermented control (enzyme containing strains 1-2783, 1-2774, 1-2835 and 1-1968) in the presence of increasing concentrations (0.5, 1.0 and 1.5 g / L) "lure" hydrolysates (Vitalarmor 950, Armor Protein, MPH955, Fonterra).
- ingredients of the peptide or protein type are simpler when they are added during the step of preparation of the dairy "mix” (powdering of the milk), before the treatment thermal sanitation (Le., 95 ° C, 8 min) and, therefore, before fermentation.
- the risk of metabolizing the active peptide is very high.
- a functional ingredient such as Lactium® (Ingredia, France) containing a bioactive peptide (fragment 91-100 of casein ⁇ S1).
- the medium was prepared by hydration of a skimmed milk powder at 120 g / L, supplemented with 1.5 g / L of Lactium® ingredient (corresponding to about 30 mg / L of bioactive peptide ⁇ S1 [91-100] ), then pasteurized at 95 ° C for 8 minutes.
- the lactic ferment was added at a rate of 0.02%, and the fermentation was conducted at the optimum temperature of the selected ferment (between 37 and 42 ° C) until a pH of 4.70 was reached.
- the sample was prepared by dilution of the fermented medium in a mixture of water, methanol and trifluoroacetic acid (50/50 / 0.1%), in a ratio of 1 to about 6.
- the supernatant after centrifugation constituted the representative sample of the peptide content of the fermented medium.
- This sample was injected into an HPLC chromatography system of the Agilent 1100 type (Agilent Technologies France, 1 rue Galvani 91745 Massy Cedex, France), equipped with a column adapted to the analysis of peptides, of the Waters Symetry® type (5 ⁇ m 2.1 x 150 mm, WAT056975, Waters France, 5, Rue Jacques Monod,
- MS / MS for example with an ion trap device such as Esquire3000 + (Bruker Daltonique, rue de l'Industrie, 67166
- the results are illustrated in FIGS. 2 and 3.
- the Lactium® ingredient contains many other peptides, some of which potentially have biological activity (such as ⁇ S1 casein fragment 23-34, which is also commercially available in the USSR).
- ingredient C12 from DMV International). It is interesting to note that almost all the peptides provided by the addition of Lactium® are widely consumed during fermentation.
- Table 3 shows that all the enzymes and strains tested metabolize from 94 to 100% of the bioactive peptide ⁇ S1 [91-100] during the fermentation of a standard dairy mix. The implementation of this ingredient is therefore impossible under conventional conditions to produce food products, including dairy, containing peptides and / or bioactive proteins in amounts sufficiently stable over time to produce an effect in the consumer.
- the C12 and CPP ingredients produced by DMV International are hydrolysates of milk proteins containing bioactive peptides targeting the control of hypertension and the assimilation of minerals respectively.
- the population of living lactic acid bacteria in the finished product continues to metabolize the bioactive peptide during storage of the finished product, so that after only 10 days (for fresh products with a 28-day DLC), between 35 and 50% of the peptide ⁇ S1 [91-100] have disappeared, which remains unacceptable to obtain the desired effect in the consumer.
- the industrial manufacturing line is more complex and requires a higher specific investment; the product no longer benefits from names related to products containing live ferments (yogurt type) and in fact loses the benefits associated with the consumption of lactic ferments;
- the strategy is to saturate the proteolytic / peptide transport systems of lactic acid bacteria by adding a sufficient amount of one or more peptides ("lure" peptides) preferred to the one to be protected.
- the protective effect exists both during fermentation and during storage of the finished product up to DLC.
- Figure 6 shows an exemplary embodiment on the model of previous tests. As shown in FIG. 6, the ⁇ S1 [91-100] peptide introduced in the form of Lactium® after fermentation is largely protected in the presence of the Vitalarmor 950 casein hydrolyzate (Armor Protein, France) compared with the control.
- Table 5 shows the consumption of the bioactive peptide ⁇ S1 [91-100] (provided by the equivalent of 1.5 g / L of Lactium®) during fermentation by the ferment containing strains I-2783, I-2774, I-2835 and 1-1968, in the presence of different commercial hydrolysates (identical concentration of 1.5 g / L).
- WPH 917 Whey Protein Hydrolyzate, NZMP Gmbh, Siemensstrasse 6-14, D-25462, Rellingen, Germany
- WPH 955 Whey Protein Hydrolyzate, NZMP Gmbh, Siemensstrasse 6-14, D-25462, Rellingen, Germany
- ArIa 20-21 whey protein hydrolyzate, ArIa Foods Ingredients Amba, 2 rue Victor Griffuelhes, 92772 Boulogne Cedex, France - WPH 926: whey protein hydrolyzate, NZMP GmbH, Siemensstrasse 6-14, D-25462, Rellingen , Germany
- DMV C 12 Dairy protein hydrolyzate, DMV INTERNATIONAL, PO Box 105, Redhill Surrey RH1 3YH, Great Britain
- the concentration of decoy peptide is also an important factor: the higher it is, the more the protection of the peptide of interest is strong, as shown in FIG. 7. More generally, it is the peptide proportion of interest. / lure peptide that regulates the more or less effective protective effect of the peptide of interest, as shown in Figure 8.
- the protection thus obtained is not specific to the peptide ⁇ S1 [91-100], but concerns the major part of the peptides of the hydrolyzate of interest. It is thus possible to protect, with a judicious choice of lure ingredient provided in sufficient quantity, any type of peptide in a wide range of size.
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Polymers & Plastics (AREA)
- Food Science & Technology (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Nutrition Science (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Biotechnology (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Tropical Medicine & Parasitology (AREA)
- Biomedical Technology (AREA)
- Virology (AREA)
- Medicinal Chemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Mycology (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Dairy Products (AREA)
- Fodder In General (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- General Preparation And Processing Of Foods (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
FR0411272A FR2876874B1 (fr) | 2004-10-22 | 2004-10-22 | Protection d'ingredients alimentaires bioactifs par l'utilisation d'ingredients leurres |
PCT/EP2005/055297 WO2006042836A1 (fr) | 2004-10-22 | 2005-10-17 | Protection d'ingrédients alimentaires bioactifs par l'utilisation d'ingrédients leurres |
Publications (1)
Publication Number | Publication Date |
---|---|
EP1802204A1 true EP1802204A1 (fr) | 2007-07-04 |
Family
ID=34952497
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
EP05794531A Withdrawn EP1802204A1 (fr) | 2004-10-22 | 2005-10-17 | Protection d'ingrédients alimentaires bioactifs par l'utilisation d'ingrédients leurres |
Country Status (9)
Country | Link |
---|---|
US (1) | US20070298144A1 (ja) |
EP (1) | EP1802204A1 (ja) |
JP (1) | JP2008516619A (ja) |
CN (1) | CN101102682A (ja) |
BR (1) | BRPI0517004A (ja) |
CA (1) | CA2584543A1 (ja) |
FR (1) | FR2876874B1 (ja) |
MX (1) | MX2007004878A (ja) |
WO (1) | WO2006042836A1 (ja) |
Families Citing this family (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
FR2876876B1 (fr) * | 2004-10-22 | 2007-02-16 | Gervais Danone Sa | Protection d'ingredients alimentaires bioactifs par l'utilisation de microorganismes presentant une capacite de metabolisation reduite |
RU2659240C2 (ru) * | 2016-05-23 | 2018-06-29 | федеральное государственное бюджетное образовательное учреждение высшего образования "Кемеровский государственный университет" (КемГУ) | Способ получения функционального продукта питания для реабилитации онкологических больных |
Family Cites Families (14)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US3878050A (en) * | 1974-04-01 | 1975-04-15 | Coors Co Adolph | Multi-differential agar culture medium |
JPH05268907A (ja) * | 1992-03-26 | 1993-10-19 | Ogawa Koryo Kk | カルシウム強化発酵タンパク組成物 |
IT1270216B (it) * | 1994-06-14 | 1997-04-29 | Recordati Chem Pharm | Metodo di stabilizzazione di composti biologicamente attivi mediante microgranuli ricoperti sospendibili in fluidi alimentari |
JP2966330B2 (ja) * | 1995-09-29 | 1999-10-25 | 雪印乳業株式会社 | 発酵乳及びその製造法 |
US5821217A (en) * | 1995-10-27 | 1998-10-13 | Beth Israel Deaconess Medical Center, Inc. | Enteral formulation: low in fat and containing protein hydrolysates |
US7190984B1 (en) * | 1996-03-05 | 2007-03-13 | Nellcor Puritan Bennett Incorporated | Shunt barrier in pulse oximeter sensor |
JP3755855B2 (ja) * | 1997-05-13 | 2006-03-15 | 日本ミルクコミュニティ株式会社 | 発酵乳及びその製造法 |
US6368591B2 (en) * | 1998-05-15 | 2002-04-09 | Shanghai Sine Pharmaceutical Corporation Ltd. | Beneficial microbe composition, new protective materials for the microbes, method to prepare the same and uses thereof |
FR2778921B1 (fr) * | 1998-05-22 | 2001-05-11 | Gervais Danone Sa | Souches mutantes de lactobacillus bulgaricus depourvues d'activite beta-galactosidase |
FI113741B (fi) * | 1999-11-01 | 2004-06-15 | Valio Oy | Menetelmä verenpainetta alentavia peptidejä sisältävän tuotteen valmistamiseksi |
JP4084916B2 (ja) * | 2000-06-21 | 2008-04-30 | 株式会社東洋新薬 | 麦若葉由来の素材を含む抗高血圧食品 |
JP3481931B2 (ja) * | 2001-01-25 | 2003-12-22 | 森永乳業株式会社 | 抗潰瘍性発酵乳及び抗潰瘍性発酵乳の製造方法 |
JP3935853B2 (ja) * | 2003-03-20 | 2007-06-27 | 株式会社ヤクルト本社 | 発酵乳およびその製造方法 |
WO2005096847A1 (en) * | 2004-03-19 | 2005-10-20 | Campina Nederland Holding B.V. | Method of preparing a food ingredient and food product having angiotensin-i-converting enzyme inhibiting properties and products thus obtained |
-
2004
- 2004-10-22 FR FR0411272A patent/FR2876874B1/fr not_active Expired - Fee Related
-
2005
- 2005-10-17 US US11/577,620 patent/US20070298144A1/en not_active Abandoned
- 2005-10-17 CN CNA2005800406160A patent/CN101102682A/zh active Pending
- 2005-10-17 CA CA002584543A patent/CA2584543A1/fr not_active Abandoned
- 2005-10-17 MX MX2007004878A patent/MX2007004878A/es unknown
- 2005-10-17 JP JP2007537259A patent/JP2008516619A/ja not_active Ceased
- 2005-10-17 WO PCT/EP2005/055297 patent/WO2006042836A1/fr active Application Filing
- 2005-10-17 EP EP05794531A patent/EP1802204A1/fr not_active Withdrawn
- 2005-10-17 BR BRPI0517004-4A patent/BRPI0517004A/pt not_active IP Right Cessation
Non-Patent Citations (1)
Title |
---|
See references of WO2006042836A1 * |
Also Published As
Publication number | Publication date |
---|---|
JP2008516619A (ja) | 2008-05-22 |
FR2876874B1 (fr) | 2007-02-16 |
CN101102682A (zh) | 2008-01-09 |
US20070298144A1 (en) | 2007-12-27 |
BRPI0517004A (pt) | 2008-09-30 |
MX2007004878A (es) | 2007-07-04 |
FR2876874A1 (fr) | 2006-04-28 |
CA2584543A1 (fr) | 2006-04-27 |
WO2006042836A1 (fr) | 2006-04-27 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
CA2584615C (fr) | Protection d'ingredients alimentaires bioactifs par l'utilisation de microorganismes presentant une capacite de metabolisation reduite | |
EP1811853A1 (fr) | Protection d'ingrédients alimentaires bioactifs par encapsulation | |
EP1802652A1 (fr) | Souches de streptococcus thermophilus ami déficientes à post-acidification réduite | |
EP2040560B1 (fr) | Granules de cysteine et leurs utilisations a titre d'activateurs de croissance de bifidobacterium animalis lactis | |
EP1991661B1 (fr) | Souches de lactobacillus helveticus ne fermentant pas le lactose | |
AU2017287989B2 (en) | Composition for use in improvement of nutritional state | |
CA2551494C (fr) | Produit alimentaire liquide comprenant des granules de bacteries lactiques | |
EP1820849B1 (fr) | Nouvelles souches de Lactobacillus helveticus | |
JP3888811B2 (ja) | Gaba含有発酵乳の製造方法 | |
EP1802204A1 (fr) | Protection d'ingrédients alimentaires bioactifs par l'utilisation d'ingrédients leurres | |
CA2346553C (fr) | Composition alimentaire a base de matiere issue de lait comprenant des glycerides d'acide linoleique conjugue | |
EP1820850B1 (fr) | Nouvelles souches de lactobacillus helveticus | |
EP1820405B1 (fr) | Nouvelles souches de Lactobacillus Helveticus |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
PUAI | Public reference made under article 153(3) epc to a published international application that has entered the european phase |
Free format text: ORIGINAL CODE: 0009012 |
|
17P | Request for examination filed |
Effective date: 20070419 |
|
AK | Designated contracting states |
Kind code of ref document: A1 Designated state(s): AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HU IE IS IT LI LT LU LV MC NL PL PT RO SE SI SK TR |
|
RAP1 | Party data changed (applicant data changed or rights of an application transferred) |
Owner name: COMPAGNIE GERVAIS DANONE |
|
DAX | Request for extension of the european patent (deleted) | ||
17Q | First examination report despatched |
Effective date: 20080507 |
|
RIN1 | Information on inventor provided before grant (corrected) |
Inventor name: BEAL, CHLOE Inventor name: SAINT DENIS, THIERRY Inventor name: PIERSON, ANNE Inventor name: COURCON, OLIVIER |
|
STAA | Information on the status of an ep patent application or granted ep patent |
Free format text: STATUS: THE APPLICATION IS DEEMED TO BE WITHDRAWN |
|
18D | Application deemed to be withdrawn |
Effective date: 20120501 |