NL8700767A - Dipeptidase, isolering daarvan uit melkzuurbacterien, antilichamen tegen het dipeptidase, gebruik van het dipeptidase en van de antilichamen daartegen. - Google Patents
Dipeptidase, isolering daarvan uit melkzuurbacterien, antilichamen tegen het dipeptidase, gebruik van het dipeptidase en van de antilichamen daartegen. Download PDFInfo
- Publication number
- NL8700767A NL8700767A NL8700767A NL8700767A NL8700767A NL 8700767 A NL8700767 A NL 8700767A NL 8700767 A NL8700767 A NL 8700767A NL 8700767 A NL8700767 A NL 8700767A NL 8700767 A NL8700767 A NL 8700767A
- Authority
- NL
- Netherlands
- Prior art keywords
- dipeptidase
- leu
- lactic acid
- enzyme
- ala
- Prior art date
Links
- 108090001081 Dipeptidases Proteins 0.000 title claims abstract description 87
- 102000004860 Dipeptidases Human genes 0.000 title claims abstract description 86
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 title claims abstract description 50
- 239000004310 lactic acid Substances 0.000 title claims abstract description 25
- 235000014655 lactic acid Nutrition 0.000 title claims abstract description 25
- 241000894006 Bacteria Species 0.000 title claims abstract description 24
- 238000009413 insulation Methods 0.000 title 1
- 108010091798 leucylleucine Proteins 0.000 claims abstract description 36
- 238000000034 method Methods 0.000 claims abstract description 25
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 25
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 19
- 239000000758 substrate Substances 0.000 claims abstract description 14
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 claims abstract description 10
- 108010050848 glycylleucine Proteins 0.000 claims abstract description 10
- 239000000203 mixture Substances 0.000 claims abstract description 9
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 claims abstract description 8
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 claims abstract description 8
- DEFJQIDDEAULHB-IMJSIDKUSA-N L-alanyl-L-alanine Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(O)=O DEFJQIDDEAULHB-IMJSIDKUSA-N 0.000 claims abstract description 6
- 108010056243 alanylalanine Proteins 0.000 claims abstract description 6
- 229910052751 metal Inorganic materials 0.000 claims abstract description 6
- 239000002184 metal Substances 0.000 claims abstract description 6
- DKEXFJVMVGETOO-LURJTMIESA-N Gly-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)CN DKEXFJVMVGETOO-LURJTMIESA-N 0.000 claims abstract description 5
- LESXFEZIFXFIQR-LURJTMIESA-N Leu-Gly Chemical compound CC(C)C[C@H](N)C(=O)NCC(O)=O LESXFEZIFXFIQR-LURJTMIESA-N 0.000 claims abstract description 5
- MDSUKZSLOATHMH-IUCAKERBSA-N Leu-Val Chemical compound CC(C)C[C@H]([NH3+])C(=O)N[C@@H](C(C)C)C([O-])=O MDSUKZSLOATHMH-IUCAKERBSA-N 0.000 claims abstract description 5
- MDSUKZSLOATHMH-UHFFFAOYSA-N N-L-leucyl-L-valine Natural products CC(C)CC(N)C(=O)NC(C(C)C)C(O)=O MDSUKZSLOATHMH-UHFFFAOYSA-N 0.000 claims abstract description 5
- RFCVXVPWSPOMFJ-STQMWFEESA-N Phe-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@@H](N)CC1=CC=CC=C1 RFCVXVPWSPOMFJ-STQMWFEESA-N 0.000 claims abstract description 5
- XCTHZFGSVQBHBW-IUCAKERBSA-N Val-Leu Chemical compound CC(C)C[C@@H](C([O-])=O)NC(=O)[C@@H]([NH3+])C(C)C XCTHZFGSVQBHBW-IUCAKERBSA-N 0.000 claims abstract description 5
- 108010073101 phenylalanylleucine Proteins 0.000 claims abstract description 5
- 108010036320 valylleucine Proteins 0.000 claims abstract description 5
- MYFMARDICOWMQP-UHFFFAOYSA-N L-L-gamma-Glutamylleucine Natural products CC(C)CC(C(O)=O)NC(=O)CCC(N)C(O)=O MYFMARDICOWMQP-UHFFFAOYSA-N 0.000 claims abstract description 4
- NTISAKGPIGTIJJ-IUCAKERBSA-N Leu-Met Chemical compound CSCC[C@@H](C(O)=O)NC(=O)[C@@H](N)CC(C)C NTISAKGPIGTIJJ-IUCAKERBSA-N 0.000 claims abstract description 4
- 125000000539 amino acid group Chemical group 0.000 claims abstract description 4
- MYFMARDICOWMQP-YUMQZZPRSA-N gamma-Glu-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)CC[C@H](N)C(O)=O MYFMARDICOWMQP-YUMQZZPRSA-N 0.000 claims abstract description 4
- 108010064169 gamma-glutamyl-leucine Proteins 0.000 claims abstract description 4
- 108010025306 histidylleucine Proteins 0.000 claims abstract description 4
- 108010091871 leucylmethionine Proteins 0.000 claims abstract description 4
- 230000035945 sensitivity Effects 0.000 claims abstract description 4
- JZDHUJAFXGNDSB-WHFBIAKZSA-N Glu-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@@H](N)CCC(O)=O JZDHUJAFXGNDSB-WHFBIAKZSA-N 0.000 claims abstract description 3
- 239000003638 chemical reducing agent Substances 0.000 claims abstract description 3
- 230000000694 effects Effects 0.000 claims description 73
- 230000007062 hydrolysis Effects 0.000 claims description 44
- 238000006460 hydrolysis reaction Methods 0.000 claims description 44
- LCPYQJIKPJDLLB-UWVGGRQHSA-N Leu-Leu Chemical compound CC(C)C[C@H](N)C(=O)N[C@H](C(O)=O)CC(C)C LCPYQJIKPJDLLB-UWVGGRQHSA-N 0.000 claims description 33
- 235000013351 cheese Nutrition 0.000 claims description 11
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 claims description 9
- 241000194034 Lactococcus lactis subsp. cremoris Species 0.000 claims description 8
- 238000010828 elution Methods 0.000 claims description 6
- 238000004440 column chromatography Methods 0.000 claims description 5
- 238000002360 preparation method Methods 0.000 claims description 5
- 235000014962 Streptococcus cremoris Nutrition 0.000 claims description 4
- 238000005342 ion exchange Methods 0.000 claims description 4
- 238000005194 fractionation Methods 0.000 claims description 2
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 claims description 2
- 235000013622 meat product Nutrition 0.000 claims 2
- 235000013305 food Nutrition 0.000 abstract description 8
- 238000004519 manufacturing process Methods 0.000 abstract description 5
- 230000003301 hydrolyzing effect Effects 0.000 abstract description 3
- 230000008569 process Effects 0.000 abstract description 3
- VHJLVAABSRFDPM-UHFFFAOYSA-N 1,4-dithiothreitol Chemical compound SCC(O)C(O)CS VHJLVAABSRFDPM-UHFFFAOYSA-N 0.000 abstract 1
- 102000004190 Enzymes Human genes 0.000 description 61
- 108090000790 Enzymes Proteins 0.000 description 61
- 229940088598 enzyme Drugs 0.000 description 61
- 102000035195 Peptidases Human genes 0.000 description 21
- 108091005804 Peptidases Proteins 0.000 description 21
- 150000001413 amino acids Chemical class 0.000 description 19
- 229940024606 amino acid Drugs 0.000 description 18
- 235000001014 amino acid Nutrition 0.000 description 18
- 235000019833 protease Nutrition 0.000 description 18
- 229920002401 polyacrylamide Polymers 0.000 description 17
- 238000001962 electrophoresis Methods 0.000 description 16
- 108090000623 proteins and genes Proteins 0.000 description 14
- 102000004169 proteins and genes Human genes 0.000 description 14
- 235000018102 proteins Nutrition 0.000 description 13
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 12
- 239000000499 gel Substances 0.000 description 12
- 239000000872 buffer Substances 0.000 description 10
- 210000004027 cell Anatomy 0.000 description 9
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 7
- 238000001502 gel electrophoresis Methods 0.000 description 7
- 230000005764 inhibitory process Effects 0.000 description 7
- 238000000746 purification Methods 0.000 description 7
- 108010016626 Dipeptides Proteins 0.000 description 6
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 6
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 6
- 239000011780 sodium chloride Substances 0.000 description 6
- 239000000126 substance Substances 0.000 description 6
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 5
- 239000007995 HEPES buffer Substances 0.000 description 5
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 5
- 229960003767 alanine Drugs 0.000 description 5
- 239000012528 membrane Substances 0.000 description 5
- 239000007858 starting material Substances 0.000 description 5
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 4
- JRBJSXQPQWSCCF-UHFFFAOYSA-N 3,3'-Dimethoxybenzidine Chemical compound C1=C(N)C(OC)=CC(C=2C=C(OC)C(N)=CC=2)=C1 JRBJSXQPQWSCCF-UHFFFAOYSA-N 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- 235000004279 alanine Nutrition 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 230000015556 catabolic process Effects 0.000 description 4
- 150000001768 cations Chemical class 0.000 description 4
- 239000003153 chemical reaction reagent Substances 0.000 description 4
- 238000002474 experimental method Methods 0.000 description 4
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 4
- 238000001155 isoelectric focusing Methods 0.000 description 4
- 229910021645 metal ion Inorganic materials 0.000 description 4
- 230000002797 proteolythic effect Effects 0.000 description 4
- 230000002829 reductive effect Effects 0.000 description 4
- 230000005070 ripening Effects 0.000 description 4
- KIUMMUBSPKGMOY-UHFFFAOYSA-N 3,3'-Dithiobis(6-nitrobenzoic acid) Chemical compound C1=C([N+]([O-])=O)C(C(=O)O)=CC(SSC=2C=C(C(=CC=2)[N+]([O-])=O)C(O)=O)=C1 KIUMMUBSPKGMOY-UHFFFAOYSA-N 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 102000004400 Aminopeptidases Human genes 0.000 description 3
- 108090000915 Aminopeptidases Proteins 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 108010053070 Glutathione Disulfide Proteins 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 235000019658 bitter taste Nutrition 0.000 description 3
- 229940098773 bovine serum albumin Drugs 0.000 description 3
- UDSAIICHUKSCKT-UHFFFAOYSA-N bromophenol blue Chemical compound C1=C(Br)C(O)=C(Br)C=C1C1(C=2C=C(Br)C(O)=C(Br)C=2)C2=CC=CC=C2S(=O)(=O)O1 UDSAIICHUKSCKT-UHFFFAOYSA-N 0.000 description 3
- 239000005018 casein Substances 0.000 description 3
- 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 description 3
- 235000021240 caseins Nutrition 0.000 description 3
- 210000002421 cell wall Anatomy 0.000 description 3
- 239000002738 chelating agent Substances 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 238000010580 coupled enzyme reaction Methods 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- YAGKRVSRTSUGEY-UHFFFAOYSA-N ferricyanide Chemical compound [Fe+3].N#[C-].N#[C-].N#[C-].N#[C-].N#[C-].N#[C-] YAGKRVSRTSUGEY-UHFFFAOYSA-N 0.000 description 3
- YPZRWBKMTBYPTK-BJDJZHNGSA-N glutathione disulfide Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(=O)NCC(O)=O)CSSC[C@@H](C(=O)NCC(O)=O)NC(=O)CC[C@H](N)C(O)=O YPZRWBKMTBYPTK-BJDJZHNGSA-N 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 230000002401 inhibitory effect Effects 0.000 description 3
- JDNTWHVOXJZDSN-UHFFFAOYSA-N iodoacetic acid Chemical compound OC(=O)CI JDNTWHVOXJZDSN-UHFFFAOYSA-N 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 108020004999 messenger RNA Proteins 0.000 description 3
- 235000013336 milk Nutrition 0.000 description 3
- 239000008267 milk Substances 0.000 description 3
- 210000004080 milk Anatomy 0.000 description 3
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 3
- BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 3
- FEMOMIGRRWSMCU-UHFFFAOYSA-N ninhydrin Chemical compound C1=CC=C2C(=O)C(O)(O)C(=O)C2=C1 FEMOMIGRRWSMCU-UHFFFAOYSA-N 0.000 description 3
- 238000001556 precipitation Methods 0.000 description 3
- 239000011541 reaction mixture Substances 0.000 description 3
- 239000012723 sample buffer Substances 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 125000003396 thiol group Chemical group [H]S* 0.000 description 3
- BJEPYKJPYRNKOW-REOHCLBHSA-N (S)-malic acid Chemical compound OC(=O)[C@@H](O)CC(O)=O BJEPYKJPYRNKOW-REOHCLBHSA-N 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 2
- JDDMPHKHKQRDPT-UHFFFAOYSA-N 3-naphthalen-1-ylpyrrole-2,5-dione Chemical compound O=C1NC(=O)C(C=2C3=CC=CC=C3C=CC=2)=C1 JDDMPHKHKQRDPT-UHFFFAOYSA-N 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 2
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- 108010024636 Glutathione Proteins 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 239000007836 KH2PO4 Substances 0.000 description 2
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 2
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 229910021380 Manganese Chloride Inorganic materials 0.000 description 2
- GLFNIEUTAYBVOC-UHFFFAOYSA-L Manganese chloride Chemical compound Cl[Mn]Cl GLFNIEUTAYBVOC-UHFFFAOYSA-L 0.000 description 2
- 102000016943 Muramidase Human genes 0.000 description 2
- 108010014251 Muramidase Proteins 0.000 description 2
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- BJEPYKJPYRNKOW-UHFFFAOYSA-N alpha-hydroxysuccinic acid Natural products OC(=O)C(O)CC(O)=O BJEPYKJPYRNKOW-UHFFFAOYSA-N 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 2
- 239000004327 boric acid Substances 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- ZPWVASYFFYYZEW-UHFFFAOYSA-L dipotassium hydrogen phosphate Chemical compound [K+].[K+].OP([O-])([O-])=O ZPWVASYFFYYZEW-UHFFFAOYSA-L 0.000 description 2
- 235000019797 dipotassium phosphate Nutrition 0.000 description 2
- 229910000396 dipotassium phosphate Inorganic materials 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 239000004325 lysozyme Substances 0.000 description 2
- 229960000274 lysozyme Drugs 0.000 description 2
- 235000010335 lysozyme Nutrition 0.000 description 2
- 239000001630 malic acid Substances 0.000 description 2
- 235000011090 malic acid Nutrition 0.000 description 2
- 239000011565 manganese chloride Substances 0.000 description 2
- 235000002867 manganese chloride Nutrition 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 230000035800 maturation Effects 0.000 description 2
- 229910000402 monopotassium phosphate Inorganic materials 0.000 description 2
- 235000019796 monopotassium phosphate Nutrition 0.000 description 2
- 235000015097 nutrients Nutrition 0.000 description 2
- YFZOUMNUDGGHIW-UHFFFAOYSA-M p-chloromercuribenzoic acid Chemical compound OC(=O)C1=CC=C([Hg]Cl)C=C1 YFZOUMNUDGGHIW-UHFFFAOYSA-M 0.000 description 2
- GNSKLFRGEWLPPA-UHFFFAOYSA-M potassium dihydrogen phosphate Chemical compound [K+].OP(O)([O-])=O GNSKLFRGEWLPPA-UHFFFAOYSA-M 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 229910052709 silver Inorganic materials 0.000 description 2
- 239000004332 silver Substances 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 230000000638 stimulation Effects 0.000 description 2
- 235000019640 taste Nutrition 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- IHPYMWDTONKSCO-UHFFFAOYSA-N 2,2'-piperazine-1,4-diylbisethanesulfonic acid Chemical compound OS(=O)(=O)CCN1CCN(CCS(O)(=O)=O)CC1 IHPYMWDTONKSCO-UHFFFAOYSA-N 0.000 description 1
- KPGXRSRHYNQIFN-UHFFFAOYSA-N 2-oxoglutaric acid Chemical compound OC(=O)CCC(=O)C(O)=O KPGXRSRHYNQIFN-UHFFFAOYSA-N 0.000 description 1
- BYXHQQCXAJARLQ-ZLUOBGJFSA-N Ala-Ala-Ala Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(O)=O BYXHQQCXAJARLQ-ZLUOBGJFSA-N 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 208000002109 Argyria Diseases 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 102000003846 Carbonic anhydrases Human genes 0.000 description 1
- 108090000209 Carbonic anhydrases Proteins 0.000 description 1
- 102100030497 Cytochrome c Human genes 0.000 description 1
- 108010075031 Cytochromes c Proteins 0.000 description 1
- QNAYBMKLOCPYGJ-UHFFFAOYSA-N D-alpha-Ala Natural products CC([NH3+])C([O-])=O QNAYBMKLOCPYGJ-UHFFFAOYSA-N 0.000 description 1
- 239000003298 DNA probe Substances 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- XPDXVDYUQZHFPV-UHFFFAOYSA-N Dansyl Chloride Chemical compound C1=CC=C2C(N(C)C)=CC=CC2=C1S(Cl)(=O)=O XPDXVDYUQZHFPV-UHFFFAOYSA-N 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- MMFKFJORZBJVNF-UWVGGRQHSA-N His-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@@H](N)CC1=CN=CN1 MMFKFJORZBJVNF-UWVGGRQHSA-N 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 102000004867 Hydro-Lyases Human genes 0.000 description 1
- 108090001042 Hydro-Lyases Proteins 0.000 description 1
- 102100034343 Integrase Human genes 0.000 description 1
- QNAYBMKLOCPYGJ-UWTATZPHSA-N L-Alanine Natural products C[C@@H](N)C(O)=O QNAYBMKLOCPYGJ-UWTATZPHSA-N 0.000 description 1
- 108010008292 L-Amino Acid Oxidase Proteins 0.000 description 1
- 102000007070 L-amino-acid oxidase Human genes 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- 102000003855 L-lactate dehydrogenase Human genes 0.000 description 1
- 108700023483 L-lactate dehydrogenases Proteins 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- VWHGTYCRDRBSFI-ZETCQYMHSA-N Leu-Gly-Gly Chemical compound CC(C)C[C@H](N)C(=O)NCC(=O)NCC(O)=O VWHGTYCRDRBSFI-ZETCQYMHSA-N 0.000 description 1
- DNDWZFHLZVYOGF-KKUMJFAQSA-N Leu-Leu-Leu Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O DNDWZFHLZVYOGF-KKUMJFAQSA-N 0.000 description 1
- 241000192132 Leuconostoc Species 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 102000014171 Milk Proteins Human genes 0.000 description 1
- 108010011756 Milk Proteins Proteins 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- YGYAWVDWMABLBF-UHFFFAOYSA-N Phosgene Chemical compound ClC(Cl)=O YGYAWVDWMABLBF-UHFFFAOYSA-N 0.000 description 1
- 108010065081 Phosphorylase b Proteins 0.000 description 1
- ZKQOUHVVXABNDG-IUCAKERBSA-N Pro-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1 ZKQOUHVVXABNDG-IUCAKERBSA-N 0.000 description 1
- 101710098398 Probable alanine aminotransferase, mitochondrial Proteins 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 241000194017 Streptococcus Species 0.000 description 1
- 244000057717 Streptococcus lactis Species 0.000 description 1
- 235000014897 Streptococcus lactis Nutrition 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 108010017893 alanyl-alanyl-alanine Proteins 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 229910000413 arsenic oxide Inorganic materials 0.000 description 1
- 229960002594 arsenic trioxide Drugs 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 235000013405 beer Nutrition 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 150000003841 chloride salts Chemical class 0.000 description 1
- 238000005352 clarification Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000012468 concentrated sample Substances 0.000 description 1
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
- 235000014048 cultured milk product Nutrition 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000013365 dairy product Nutrition 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 230000006866 deterioration Effects 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 125000002228 disulfide group Chemical group 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000001952 enzyme assay Methods 0.000 description 1
- 239000006167 equilibration buffer Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 238000000760 immunoelectrophoresis Methods 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 238000010983 kinetics study Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 108010044311 leucyl-glycyl-glycine Proteins 0.000 description 1
- 108010049589 leucyl-leucyl-leucine Proteins 0.000 description 1
- 229940072783 liquimat Drugs 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 235000021239 milk protein Nutrition 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 239000006872 mrs medium Substances 0.000 description 1
- VBEGHXKAFSLLGE-UHFFFAOYSA-N n-phenylnitramide Chemical compound [O-][N+](=O)NC1=CC=CC=C1 VBEGHXKAFSLLGE-UHFFFAOYSA-N 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- YPZRWBKMTBYPTK-UHFFFAOYSA-N oxidized gamma-L-glutamyl-L-cysteinylglycine Natural products OC(=O)C(N)CCC(=O)NC(C(=O)NCC(O)=O)CSSCC(C(=O)NCC(O)=O)NC(=O)CCC(N)C(O)=O YPZRWBKMTBYPTK-UHFFFAOYSA-N 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 229960005190 phenylalanine Drugs 0.000 description 1
- 235000008729 phenylalanine Nutrition 0.000 description 1
- IEKVHGDUBCZHRB-UHFFFAOYSA-N phenylarsenic Chemical compound [As]C1=CC=CC=C1 IEKVHGDUBCZHRB-UHFFFAOYSA-N 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 108010090894 prolylleucine Proteins 0.000 description 1
- 238000002731 protein assay Methods 0.000 description 1
- 238000009790 rate-determining step (RDS) Methods 0.000 description 1
- 230000007420 reactivation Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 235000020183 skimmed milk Nutrition 0.000 description 1
- 235000014214 soft drink Nutrition 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 239000003774 sulfhydryl reagent Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 230000007306 turnover Effects 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 239000011592 zinc chloride Substances 0.000 description 1
- 235000005074 zinc chloride Nutrition 0.000 description 1
- JIAARYAFYJHUJI-UHFFFAOYSA-L zinc dichloride Chemical compound [Cl-].[Cl-].[Zn+2] JIAARYAFYJHUJI-UHFFFAOYSA-L 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/13—Dipeptidases (3.4.13)
- C12Y304/13011—Dipeptidase (3.4.13.11)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/40—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against enzymes
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
-
- 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
- A23V2400/215—Cremoris
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/814—Enzyme separation or purification
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/8215—Microorganisms
- Y10S435/822—Microorganisms using bacteria or actinomycetales
- Y10S435/853—Lactobacillus
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- General Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Immunology (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Dairy Products (AREA)
Priority Applications (10)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| NL8700767A NL8700767A (nl) | 1987-04-01 | 1987-04-01 | Dipeptidase, isolering daarvan uit melkzuurbacterien, antilichamen tegen het dipeptidase, gebruik van het dipeptidase en van de antilichamen daartegen. |
| DK171888A DK171888A (da) | 1987-04-01 | 1988-03-29 | Dipeptidase, fremgangsmaade til isolering deraf og anvendelse |
| IE96988A IE63958B1 (en) | 1987-04-01 | 1988-03-31 | Dipeptidase its isolation from lactic acid bacteria antibodies against the dipeptidase the use of the dipeptidase and of the antibodies against it |
| ES88200607T ES2067463T3 (es) | 1987-04-01 | 1988-03-31 | Dipeptidasa de bacterias acidolacticas en forma aislada. |
| EP88200607A EP0286171B1 (en) | 1987-04-01 | 1988-03-31 | Dipeptidase, its isolation from lactic acid bacteria, antibodies against the dipeptidase, the use of the dipeptidase and of the antibodies against it |
| US07/175,768 US4888284A (en) | 1987-04-01 | 1988-03-31 | Dipeptidase, its isolation from lactic acid bacteria, antibodies against the dipeptidase, the use of the dipeptidase and of the antibodies against it |
| DE88200607T DE3879740T2 (de) | 1987-04-01 | 1988-03-31 | Dipeptidase, deren Isolierung aus Milchsäure-Bakterien, Immunkörper gegen diese Dipeptidase, Verwendung dieser Dipeptidase und dieser Immunkörper. |
| AT88200607T ATE87652T1 (de) | 1987-04-01 | 1988-03-31 | Dipeptidase, deren isolierung aus milchsaeurebakterien, immunkoerper gegen diese dipeptidase, verwendung dieser dipeptidase und dieser immunkoerper. |
| CA000563088A CA1311203C (en) | 1987-04-01 | 1988-03-31 | Dipeptidase, its isolation from lactic acid bacteria, antibodies against the dipeptidase, the use of the dipeptidase and of the antibodies against it |
| JP63078333A JPS6420085A (en) | 1987-04-01 | 1988-04-01 | Dipeptidase, isolation thereof from lactic bacteria and anti-dipeptidase antibody |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| NL8700767 | 1987-04-01 | ||
| NL8700767A NL8700767A (nl) | 1987-04-01 | 1987-04-01 | Dipeptidase, isolering daarvan uit melkzuurbacterien, antilichamen tegen het dipeptidase, gebruik van het dipeptidase en van de antilichamen daartegen. |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NL8700767A true NL8700767A (nl) | 1988-11-01 |
Family
ID=19849795
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NL8700767A NL8700767A (nl) | 1987-04-01 | 1987-04-01 | Dipeptidase, isolering daarvan uit melkzuurbacterien, antilichamen tegen het dipeptidase, gebruik van het dipeptidase en van de antilichamen daartegen. |
Country Status (10)
| Country | Link |
|---|---|
| US (1) | US4888284A (da) |
| EP (1) | EP0286171B1 (da) |
| JP (1) | JPS6420085A (da) |
| AT (1) | ATE87652T1 (da) |
| CA (1) | CA1311203C (da) |
| DE (1) | DE3879740T2 (da) |
| DK (1) | DK171888A (da) |
| ES (1) | ES2067463T3 (da) |
| IE (1) | IE63958B1 (da) |
| NL (1) | NL8700767A (da) |
Families Citing this family (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| NL8901994A (nl) * | 1989-08-02 | 1991-03-01 | Dmv Campina Bv | Aminopeptidase. |
| FR2651328B1 (fr) * | 1989-08-31 | 1993-03-26 | Agronomique Inst Nat Rech | Reactifs et methodes immunochimiques pour la mesure de la croissance des microorganismes et de la quantite de proteines au cours d'une fermentation industrielle. |
| SK138197A3 (en) | 1995-04-11 | 1998-07-08 | Merck & Co Inc | Bioprocess for production of dipeptide based compounds |
| US6103468A (en) * | 1997-10-07 | 2000-08-15 | Labatt Brewing Company Limited | Rapid two-stage polymerase chain reaction method for detection of lactic acid bacteria in beer |
| US8263144B2 (en) * | 2005-11-17 | 2012-09-11 | Kraft Foods Global Brands Llc | Cheese flavor composition and process for making same |
| ES2545873T3 (es) * | 2013-05-23 | 2015-09-16 | Bruker Daltonik Gmbh | Determinación de resistencia con espectrometría de masas mediante la medición de la proliferación microbiana |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3947324A (en) * | 1975-04-21 | 1976-03-30 | G. D. Searle And Co. | Method for isolating high purity peroxidase |
| US4233387A (en) * | 1979-03-05 | 1980-11-11 | Xerox Corporation | Electrophotographic carrier powder coated by resin dry-mixing process |
| JPS58209980A (ja) * | 1982-04-27 | 1983-12-07 | Kyowa Hakko Kogyo Co Ltd | 酵素の精製法 |
| NL8400687A (nl) * | 1984-03-02 | 1985-10-01 | Unilever Nv | Recombinant plasmiden; recombinant plasmiden bevattende bacterien; werkwijze voor het bereiden of vervaardigen van een zuivelproduct; werkwijze voor het bereiden van een eiwit. |
-
1987
- 1987-04-01 NL NL8700767A patent/NL8700767A/nl not_active Application Discontinuation
-
1988
- 1988-03-29 DK DK171888A patent/DK171888A/da not_active IP Right Cessation
- 1988-03-31 AT AT88200607T patent/ATE87652T1/de not_active IP Right Cessation
- 1988-03-31 CA CA000563088A patent/CA1311203C/en not_active Expired - Lifetime
- 1988-03-31 US US07/175,768 patent/US4888284A/en not_active Expired - Fee Related
- 1988-03-31 IE IE96988A patent/IE63958B1/en not_active IP Right Cessation
- 1988-03-31 ES ES88200607T patent/ES2067463T3/es not_active Expired - Lifetime
- 1988-03-31 DE DE88200607T patent/DE3879740T2/de not_active Expired - Fee Related
- 1988-03-31 EP EP88200607A patent/EP0286171B1/en not_active Expired - Lifetime
- 1988-04-01 JP JP63078333A patent/JPS6420085A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| JPS6420085A (en) | 1989-01-24 |
| IE880969L (en) | 1988-10-01 |
| US4888284A (en) | 1989-12-19 |
| EP0286171A1 (en) | 1988-10-12 |
| ES2067463T3 (es) | 1995-04-01 |
| CA1311203C (en) | 1992-12-08 |
| DE3879740T2 (de) | 1993-10-28 |
| DK171888D0 (da) | 1988-03-29 |
| ATE87652T1 (de) | 1993-04-15 |
| DE3879740D1 (de) | 1993-05-06 |
| DK171888A (da) | 1988-10-02 |
| EP0286171B1 (en) | 1993-03-31 |
| IE63958B1 (en) | 1995-06-28 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Van Boven et al. | Purification and characterization of a dipeptidase from Streptococcus cremoris Wg2 | |
| Khalid et al. | Purification and partial characterization of a prolyl-dipeptidyl aminopeptidase from Lactobacillus helveticus CNRZ 32 | |
| Murakami et al. | Studies on proteinases from the digestive organs of sardine. I. Purification and characterization of three alkaline proteinases from the pyloric caeca | |
| Gobbetti et al. | The proteolytic system of Lactobacillus sanfrancisco CB1: purification and characterization of a proteinase, a dipeptidase, and an aminopeptidase | |
| Neviani et al. | Purification and characterization of an aminopeptidase from Lactococcus lactis subsp. cremoris AM2 | |
| Baankreis et al. | Characterisation of a Peptidase from Lactococcus Lactis Ssp* Cremoris HP That Hydrolyses Di-and Tripeptides Containing Proline or Hydrophobic Residues as the Aminoterminal Amino Acid | |
| Bosman et al. | Purification and characterization of a tripeptidase from Lactococcus lactis subsp. cremoris Wg2 | |
| Kaminogawa et al. | Isolation and characterization of a prolidase from Streptococcus cremoris H61 | |
| Bockelmann et al. | Purification and characterization of the X-prolyl-dipeptidyl-aminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus and Lactobacillus acidophilus | |
| Miyakawa et al. | Purification and characterization of an X-prolyl dipeptidyl aminopeptidase from Lactobacillus delbrueckii ssp. bulgaricus LBU-147 | |
| McCaman et al. | Structural and catalytic properties of peptidase N from Escherichia coli K-12 | |
| NL8700767A (nl) | Dipeptidase, isolering daarvan uit melkzuurbacterien, antilichamen tegen het dipeptidase, gebruik van het dipeptidase en van de antilichamen daartegen. | |
| Tan et al. | Purification and characterization of a dipeptidase from Lactobacillus helveticus SBT 2171 | |
| EP0415470B1 (en) | Aminopeptidase | |
| Fuke et al. | The purification and characterization of prolyl aminopeptidase from Penicillium camemberti | |
| Habibi-Najafi et al. | Purification and characterization of proline iminopeptidase from Lactobacillus casei ssp. casei LLG | |
| Fernandez-Espla et al. | Purification and characterization of a dipeptidase from Lactobacillus casei ssp. casei IFPL 731 isolated from goat cheese made from raw milk | |
| Lee et al. | Purification and properties of an extracellular leucine aminopeptidase from the Bacillus sp. N2 | |
| Patel et al. | Physicochemical properties of heat-stable proteases from psychrotrophic pseudomonads | |
| Simitsopoulou et al. | Purification and partial characterization of a tripeptidase from Pediococcus pentosaceus K9. 2 | |
| Bockelmann et al. | Purification and characterization of a new tripeptidase from Lactobacillus delbrueckii ssp. bulgaricus B14 | |
| EP0522203A1 (en) | Protein from lactic acid bacteria | |
| Fernandez-Espla et al. | Purification and characterization of X-prolyl dipeptidyl aminopeptidase from Propionibacterium shermanii NCDO 853 | |
| Cheng et al. | Purification and some properties of an aminopeptidase from Bifidobacterium breve | |
| NL9000241A (nl) | Tripeptidase. |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A1B | A search report has been drawn up | ||
| BV | The patent application has lapsed |