CN108342425A - A kind of method that enzymatic conversion method prepares DL-cysteine - Google Patents
A kind of method that enzymatic conversion method prepares DL-cysteine Download PDFInfo
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- CN108342425A CN108342425A CN201810442618.1A CN201810442618A CN108342425A CN 108342425 A CN108342425 A CN 108342425A CN 201810442618 A CN201810442618 A CN 201810442618A CN 108342425 A CN108342425 A CN 108342425A
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- XUJNEKJLAYXESH-UHFFFAOYSA-N Cysteine Chemical compound SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 title claims abstract description 89
- 238000006243 chemical reaction Methods 0.000 title claims abstract description 86
- 238000000034 method Methods 0.000 title claims abstract description 33
- 230000002255 enzymatic effect Effects 0.000 title claims abstract description 12
- 229940078469 dl- cysteine Drugs 0.000 title claims description 41
- 230000008878 coupling Effects 0.000 claims abstract description 7
- 238000010168 coupling process Methods 0.000 claims abstract description 7
- 238000005859 coupling reaction Methods 0.000 claims abstract description 7
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 claims description 48
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 36
- MTCFGRXMJLQNBG-UWTATZPHSA-N D-Serine Chemical compound OC[C@@H](N)C(O)=O MTCFGRXMJLQNBG-UWTATZPHSA-N 0.000 claims description 20
- 230000000694 effects Effects 0.000 claims description 20
- 239000012530 fluid Substances 0.000 claims description 20
- 210000001082 somatic cell Anatomy 0.000 claims description 20
- 108010075344 Tryptophan synthase Proteins 0.000 claims description 19
- 239000004471 Glycine Substances 0.000 claims description 18
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 claims description 16
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 15
- AYFVYJQAPQTCCC-STHAYSLISA-N D-threonine Chemical compound C[C@H](O)[C@@H](N)C(O)=O AYFVYJQAPQTCCC-STHAYSLISA-N 0.000 claims description 14
- 102000004190 Enzymes Human genes 0.000 claims description 14
- 108090000790 Enzymes Proteins 0.000 claims description 14
- 102000001390 Fructose-Bisphosphate Aldolase Human genes 0.000 claims description 14
- 108010068561 Fructose-Bisphosphate Aldolase Proteins 0.000 claims description 14
- 239000007788 liquid Substances 0.000 claims description 14
- 239000002253 acid Substances 0.000 claims description 12
- HYHCSLBZRBJJCH-UHFFFAOYSA-M sodium hydrosulfide Chemical compound [Na+].[SH-] HYHCSLBZRBJJCH-UHFFFAOYSA-M 0.000 claims description 12
- 102000006534 Amino Acid Isomerases Human genes 0.000 claims description 11
- 108010008830 Amino Acid Isomerases Proteins 0.000 claims description 11
- 239000000758 substrate Substances 0.000 claims description 11
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 claims description 9
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 claims description 8
- 241000588724 Escherichia coli Species 0.000 claims description 8
- HZUKSQHMCTUZJL-UHFFFAOYSA-N P(=O)(O)(O)OCC=1C(=C(C(=NC1)C)O)C=O.P(=O)(O)(O)OC=1C(=NC=C(C1C=O)CO)C Chemical compound P(=O)(O)(O)OCC=1C(=C(C(=NC1)C)O)C=O.P(=O)(O)(O)OC=1C(=NC=C(C1C=O)CO)C HZUKSQHMCTUZJL-UHFFFAOYSA-N 0.000 claims description 8
- 241000589776 Pseudomonas putida Species 0.000 claims description 8
- 241000589636 Xanthomonas campestris Species 0.000 claims description 8
- 238000007664 blowing Methods 0.000 claims description 8
- 238000005119 centrifugation Methods 0.000 claims description 8
- 239000007864 aqueous solution Substances 0.000 claims description 7
- 230000001580 bacterial effect Effects 0.000 claims description 6
- 239000001963 growth medium Substances 0.000 claims description 6
- 229910021529 ammonia Inorganic materials 0.000 claims description 5
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 claims description 4
- 150000001413 amino acids Chemical class 0.000 claims description 4
- 229910052799 carbon Inorganic materials 0.000 claims description 4
- 239000000284 extract Substances 0.000 claims description 4
- 229910052757 nitrogen Inorganic materials 0.000 claims description 4
- 102000004879 Racemases and epimerases Human genes 0.000 claims description 3
- 108090001066 Racemases and epimerases Proteins 0.000 claims description 3
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 claims description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 claims description 2
- 244000068988 Glycine max Species 0.000 claims description 2
- 235000010469 Glycine max Nutrition 0.000 claims description 2
- 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 claims description 2
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 claims description 2
- 239000001888 Peptone Substances 0.000 claims description 2
- 108010080698 Peptones Proteins 0.000 claims description 2
- 229930006000 Sucrose Natural products 0.000 claims description 2
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 claims description 2
- 240000008042 Zea mays Species 0.000 claims description 2
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 claims description 2
- 235000002017 Zea mays subsp mays Nutrition 0.000 claims description 2
- 235000015278 beef Nutrition 0.000 claims description 2
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 claims description 2
- GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 claims description 2
- 229940041514 candida albicans extract Drugs 0.000 claims description 2
- 235000005822 corn Nutrition 0.000 claims description 2
- 239000008103 glucose Substances 0.000 claims description 2
- 239000008101 lactose Substances 0.000 claims description 2
- 239000002609 medium Substances 0.000 claims description 2
- 230000003647 oxidation Effects 0.000 claims description 2
- 238000007254 oxidation reaction Methods 0.000 claims description 2
- 235000019319 peptone Nutrition 0.000 claims description 2
- 239000005720 sucrose Substances 0.000 claims description 2
- 239000012138 yeast extract Substances 0.000 claims description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 abstract description 20
- 235000018417 cysteine Nutrition 0.000 abstract description 8
- 230000008901 benefit Effects 0.000 abstract description 5
- 238000000926 separation method Methods 0.000 abstract description 5
- 238000004519 manufacturing process Methods 0.000 abstract description 4
- 238000005352 clarification Methods 0.000 abstract description 3
- 238000000605 extraction Methods 0.000 abstract description 3
- 239000013067 intermediate product Substances 0.000 abstract description 3
- 150000001945 cysteines Chemical class 0.000 abstract 2
- 238000009776 industrial production Methods 0.000 abstract 1
- 230000009466 transformation Effects 0.000 abstract 1
- 239000000243 solution Substances 0.000 description 31
- LEVWYRKDKASIDU-UHFFFAOYSA-N cystine Chemical compound OC(=O)C(N)CSSCC(N)C(O)=O LEVWYRKDKASIDU-UHFFFAOYSA-N 0.000 description 18
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 16
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 15
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 12
- 239000000706 filtrate Substances 0.000 description 12
- 239000007791 liquid phase Substances 0.000 description 12
- 239000006228 supernatant Substances 0.000 description 12
- 229960002433 cysteine Drugs 0.000 description 9
- DWNBOPVKNPVNQG-LURJTMIESA-N (2s)-4-hydroxy-2-(propylamino)butanoic acid Chemical compound CCCN[C@H](C(O)=O)CCO DWNBOPVKNPVNQG-LURJTMIESA-N 0.000 description 8
- 230000008859 change Effects 0.000 description 8
- 235000019441 ethanol Nutrition 0.000 description 8
- 230000006340 racemization Effects 0.000 description 8
- RWSOTUBLDIXVET-UHFFFAOYSA-N Dihydrogen sulfide Chemical compound S RWSOTUBLDIXVET-UHFFFAOYSA-N 0.000 description 7
- 229910000037 hydrogen sulfide Inorganic materials 0.000 description 7
- 230000008569 process Effects 0.000 description 7
- 150000003839 salts Chemical class 0.000 description 7
- 238000005406 washing Methods 0.000 description 7
- WFDIJRYMOXRFFG-UHFFFAOYSA-N Acetic anhydride Chemical compound CC(=O)OC(C)=O WFDIJRYMOXRFFG-UHFFFAOYSA-N 0.000 description 6
- 235000011114 ammonium hydroxide Nutrition 0.000 description 6
- 239000012043 crude product Substances 0.000 description 6
- 238000010438 heat treatment Methods 0.000 description 6
- 230000010355 oscillation Effects 0.000 description 6
- 239000002244 precipitate Substances 0.000 description 6
- 235000011121 sodium hydroxide Nutrition 0.000 description 6
- 238000003828 vacuum filtration Methods 0.000 description 6
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 5
- 230000009467 reduction Effects 0.000 description 5
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 4
- 239000004201 L-cysteine Substances 0.000 description 4
- 235000013878 L-cysteine Nutrition 0.000 description 4
- 238000001514 detection method Methods 0.000 description 4
- 230000005611 electricity Effects 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- IFQSXNOEEPCSLW-UHFFFAOYSA-N (1-carboxy-2-sulfanylethyl)azanium;chloride Chemical compound Cl.SCC(N)C(O)=O IFQSXNOEEPCSLW-UHFFFAOYSA-N 0.000 description 3
- PWKSKIMOESPYIA-UHFFFAOYSA-N 2-acetamido-3-sulfanylpropanoic acid Chemical compound CC(=O)NC(CS)C(O)=O PWKSKIMOESPYIA-UHFFFAOYSA-N 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
- UHOVQNZJYSORNB-UHFFFAOYSA-N Benzene Chemical compound C1=CC=CC=C1 UHOVQNZJYSORNB-UHFFFAOYSA-N 0.000 description 3
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical group C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 3
- 229940024606 amino acid Drugs 0.000 description 3
- 235000001014 amino acid Nutrition 0.000 description 3
- 239000013078 crystal Substances 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 239000002994 raw material Substances 0.000 description 3
- 229910052708 sodium Inorganic materials 0.000 description 3
- 239000011734 sodium Substances 0.000 description 3
- NOWKCMXCCJGMRR-UHFFFAOYSA-N Aziridine Chemical compound C1CN1 NOWKCMXCCJGMRR-UHFFFAOYSA-N 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- SIKJAQJRHWYJAI-UHFFFAOYSA-N Indole Chemical compound C1=CC=C2NC=CC2=C1 SIKJAQJRHWYJAI-UHFFFAOYSA-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
- UCKMPCXJQFINFW-UHFFFAOYSA-N Sulphide Chemical compound [S-2] UCKMPCXJQFINFW-UHFFFAOYSA-N 0.000 description 2
- VLSOAXRVHARBEQ-UHFFFAOYSA-N [4-fluoro-2-(hydroxymethyl)phenyl]methanol Chemical compound OCC1=CC=C(F)C=C1CO VLSOAXRVHARBEQ-UHFFFAOYSA-N 0.000 description 2
- 229960000583 acetic acid Drugs 0.000 description 2
- PGZUFTROELAOMP-UHFFFAOYSA-N aziridine-2-carbonitrile Chemical compound N#CC1CN1 PGZUFTROELAOMP-UHFFFAOYSA-N 0.000 description 2
- 230000003197 catalytic effect Effects 0.000 description 2
- 238000002425 crystallisation Methods 0.000 description 2
- XBDQKXXYIPTUBI-UHFFFAOYSA-N dimethylselenoniopropionate Natural products CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 description 2
- 238000005868 electrolysis reaction Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000000855 fermentation Methods 0.000 description 2
- 230000004151 fermentation Effects 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 231100000614 poison Toxicity 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- MNWBNISUBARLIT-UHFFFAOYSA-N sodium cyanide Chemical compound [Na+].N#[C-] MNWBNISUBARLIT-UHFFFAOYSA-N 0.000 description 2
- DYIWNHDWULMNDT-UHFFFAOYSA-N 1-bromoaziridine Chemical class BrN1CC1 DYIWNHDWULMNDT-UHFFFAOYSA-N 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N L-cystine Chemical compound [O-]C(=O)[C@@H]([NH3+])CSSC[C@H]([NH3+])C([O-])=O LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- 239000005864 Sulphur Substances 0.000 description 1
- 206010053615 Thermal burn Diseases 0.000 description 1
- 208000025865 Ulcer Diseases 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- -1 aliphatic amino acid Chemical class 0.000 description 1
- HIVLDXAAFGCOFU-UHFFFAOYSA-N ammonium hydrosulfide Chemical compound [NH4+].[SH-] HIVLDXAAFGCOFU-UHFFFAOYSA-N 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 230000003078 antioxidant effect Effects 0.000 description 1
- 150000003934 aromatic aldehydes Chemical class 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 206010006451 bronchitis Diseases 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- 229960003067 cystine Drugs 0.000 description 1
- 230000002498 deadly effect Effects 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000004043 dyeing Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 235000015203 fruit juice Nutrition 0.000 description 1
- 239000012362 glacial acetic acid Substances 0.000 description 1
- 230000003648 hair appearance Effects 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 125000004435 hydrogen atom Chemical class [H]* 0.000 description 1
- JGJLWPGRMCADHB-UHFFFAOYSA-N hypobromite Inorganic materials Br[O-] JGJLWPGRMCADHB-UHFFFAOYSA-N 0.000 description 1
- 239000005457 ice water Substances 0.000 description 1
- PZOUSPYUWWUPPK-UHFFFAOYSA-N indole Natural products CC1=CC=CC2=C1C=CN2 PZOUSPYUWWUPPK-UHFFFAOYSA-N 0.000 description 1
- RKJUIXBNRJVNHR-UHFFFAOYSA-N indolenine Natural products C1=CC=C2CC=NC2=C1 RKJUIXBNRJVNHR-UHFFFAOYSA-N 0.000 description 1
- 150000002475 indoles Chemical class 0.000 description 1
- 239000003317 industrial substance Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- JKQOBWVOAYFWKG-UHFFFAOYSA-N molybdenum trioxide Chemical compound O=[Mo](=O)=O JKQOBWVOAYFWKG-UHFFFAOYSA-N 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 230000009965 odorless effect Effects 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000002574 poison Substances 0.000 description 1
- 230000007096 poisonous effect Effects 0.000 description 1
- 235000019260 propionic acid Nutrition 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- IUVKMZGDUIUOCP-BTNSXGMBSA-N quinbolone Chemical compound O([C@H]1CC[C@H]2[C@H]3[C@@H]([C@]4(C=CC(=O)C=C4CC3)C)CC[C@@]21C)C1=CCCC1 IUVKMZGDUIUOCP-BTNSXGMBSA-N 0.000 description 1
- 238000007142 ring opening reaction Methods 0.000 description 1
- KKCBUQHMOMHUOY-UHFFFAOYSA-N sodium oxide Chemical compound [O-2].[Na+].[Na+] KKCBUQHMOMHUOY-UHFFFAOYSA-N 0.000 description 1
- 229910001948 sodium oxide Inorganic materials 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 231100000397 ulcer Toxicity 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P13/00—Preparation of nitrogen-containing organic compounds
- C12P13/04—Alpha- or beta- amino acids
- C12P13/12—Methionine; Cysteine; Cystine
Landscapes
- Organic Chemistry (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Life Sciences & Earth Sciences (AREA)
- Wood Science & Technology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Microbiology (AREA)
- General Chemical & Material Sciences (AREA)
- Biotechnology (AREA)
- Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
The invention belongs to biotechnologies, and in particular to a kind of method that enzymatic conversion method prepares DL cysteines.This method has obtained the higher DL cysteines of added value using multienzyme is coupling catalysed, eliminate intermediate product separation and Extraction process, solve cheap serine during enzymatic clarification cysteine simultaneously carrys out source problem, has many advantages, such as that production cost is low, transformation time is short, easy to operate, suitable large-scale industrial production.
Description
One, technical field
The invention belongs to biotechnologies, and in particular to a kind of method that enzymatic conversion method prepares DL-cysteine.
Two, background technology
Cysteine chemical name is 2- amino-3-mercaptopropionic acids, molecular formula C3H7NO2S, relative molecular mass 121.12.
Cysteine belongs to aliphatic amino acid, and white crystalline powder is odorless, sour, is easily aoxidized, soluble easily in water, is slightly soluble in
Ethyl alcohol, insoluble in organic reagents such as ether, benzene.According to configuration difference, cysteine divides D types, L-type and the DL types, wherein DL types to be
The racemic modification of cysteine.
DL-cysteine tool has been widely used：In cosmetic field, DL-cysteine or its salt can be used for hair dyeing and scalds
Hair, has many advantages, such as not damage hair quality, naturally bright；In field of medicaments, DL-cysteine and its derivative can be used for liver solution
Poison, treatment ulcer, sets up, is infused at antipyretic-antalgic, it is especially useful in treatment bronchitis；In terms of food, half Guangs of DL-
Propylhomoserin can be used as the nourishing additive agent etc. of the antioxidant and stabilizer, animal food of fermentation assistant, milk powder and fruit juice.
Currently, the preparation method of DL-cysteine mainly has neutralization crystallisation, chemical synthesis and change according to the literature
Learn racemization method.
1, crystallisation is neutralized
DL-cysteine hydrochloric acid salt crystal is added water to be configured to a certain concentration by Chen Shian (CN 102260202A), utilizes hydrogen
Sodium oxide molybdena is neutralized to pH 6.0, reacts condensing crystallizing after 2h, and drying obtains DL-cysteine crystal.This method is simple for process, imitates
Rate is high, but the DL-cysteine hydrochloric acid salt crystal for how obtaining high-quality is crucial.
2, chemical synthesis
The bromo- azacyclopropanes of 2-, the bromo- rings of 2- is obtained by the reaction with bromine water using azacyclopropane in warm Jian Hua (CN 102531980B)
2- cyano-azacyclopropane is obtained by the reaction with Cymag in ethyleneimine, and 2- cyano-azacyclopropane obtains 2- sulphur with vulcanized sodium ring-opening reaction
Base -3- aminopropan cyanogen, last sour water solution obtain DL-cysteine.Not only step is more for chemical synthesis, but also exists secondary anti-
It answers, deadly poisonous compound Cymag is used in the technique, safety and environmentally friendly risk are big.
3, chemical racemization method
What Quan (amino acid and living resources, 2005,27 (3):55~57) using in the pure acetic acid solvent plus side of acetic anhydride
Method carries out Study on Racemization to several amino acid such as L-cysteine, and racemization rate is up to 100%, racemization rate and temperature, acetic anhydride
The correlations such as dosage and amino acid structure.
Chen Shian (CN 102887842A) is by L-cysteine hydrochloride, glacial acetic acid, propionic acid and acetone with 1:1:2:3
Ratio mixes, and 80 DEG C of reaction 1h add the aromatic aldehyde that weight is L-cysteine hydrochloride 1/4, kept the temperature after stirring evenly quiet
Reaction 8h is set, is added and is crystallized with the isometric ice water of reaction solution, cooling, is dried after ethyl alcohol washing, obtains DL-cysteine
Hydrochloride.
Chemical racemization method will use the reaction conditions such as acid, organic solvent, high temperature, and environmental protection pressure is big；And reaction process is multiple
Miscellaneous, yield is low, and there are certain difficulty for product separation.
Enzymatic conversion method because, reaction condition strong with specificity is mild, advantages of environment protection due to be paid more and more attention.Enzyme process
Conversion prepares cysteine and becomes the focus of people's research in recent years, wherein it is tryptophan synthetase to study more enzyme.Color ammonia
Acid enzyme can not only be catalyzed Serine and indole synthesis L-Trp, moreover it is possible to be catalyzed Serine and NaHS reaction
Generate L-cysteine.
Ken-ichi Ishiwata(Journal of Fermentation and Bioengineering,67(3):
169~172,1989) using Serine and NaHS as substrate, tryptophan synthetase enzymatic clarification L-cysteine,
L-cysteine reaches 114g/L in reaction solution under optimum condition, and conversion ratio is using Serine and indoles as substrate enzymatic clarification
The 47% of L-Trp.Japan Patent (JP 62215396-A, 1987；JP 63007790-A, 1988) it reports with L- ammonia
Acid is substrate, using hydrogen sulfide or sulfohydrate or sulfide as sulfydryl donor, tryptophan synthetase producing L cysteine with enzyme
Technique.
Japan Patent (JP 62019098-A, 1987) uses tryptophan synthetase using DL-serine and sulfide as substrate
Serine is converted into L-cysteine, while separation is prepared for D-Ser.
It is substrate that the report of the above tryptophan synthetase producing L cysteine with enzyme, which is using serine sterling, is existed
The problem of have：Substrate serine is of high cost, if expecting that DL-cysteine is also needed to product L-cysteine racemization.Cause
This, will realize that enzyme process prepares DL-cysteine and the cheap source of solution substrate serine and the racemization of L-cysteine is needed to ask
Topic.
Three, invention content
It is an object of the invention to avoid above-mentioned shortcoming in the prior art, a kind of efficient, low cost preparation is provided
The method of DL-cysteine.The present invention can reach by the following technical programs：
A kind of method that enzymatic conversion method prepares DL-cysteine, feature are made of following steps：
(1) by bacterial strain of the Xanthomonas campestris source with D-Thr aldolase activity, pseudomonas putida source with ammonia
There is bacterial strain, the Escherichia coli of base acid Racemase activity the active bacterial strain of tryptophan synthetase to train in the medium respectively
It supports, generates D-Thr aldolase, amino acid racemase, the tryptophan synthetase of high activity respectively；
(2) using the glycine of 50~180g/L as substrate, be added with D-Thr aldolase activity somatic cells or
Enzyme extract, the phosphopyridoxal pyridoxal phosphate of 0.05~0.5g/L, 20~40 DEG C, stream adds the formalin of 100~370g/L, uses hydrogen-oxygen
Change sodium water solution and control pH 6~9, enzymatic converts to obtain D-Ser；
(3) D-Ser conversion fluid removes somatic cells through centrifugation, and NaHS is added, and 7~10,30~50 DEG C of pH adds
Enter amino acid racemase somatic cells or crude enzyme liquid, tryptophan synthetase somatic cells or crude enzyme liquid, dual-enzyme coupling catalyze and synthesize
DL-cysteine；
(4) by the DL-cysteine blowing air of generation or dropwise addition hydrogen peroxide oxidation, the isolated DL- of isoelectric point crystallizing method
Cystine, then DL-cysteine is made through electroreduction.
Culture medium carbon source uses glucose, maltose, sucrose and/or lactose in above-mentioned steps (1), total carbon source in culture medium
Mass concentration is 1~20g/L；Nitrogen source uses beef extract, yeast extract, corn steep liquor, peptone and/or soya-bean cake hydrolyzate, culture medium
In total nitrogen source mass concentration be 1~20g/L；
Formaldehyde final concentration is not higher than 5g/L in control reaction system when stream adds formalin in above-mentioned steps (2)；
The NaHS being added in above-mentioned steps (3) can use ammonium hydro sulfide or vulcanized sodium to substitute.
The present invention catalyzes and synthesizes D-Ser using glycine and formaldehyde as raw material, first with D-Thr aldolase, then with
D-Ser and NaHS are substrate, and half Guangs of DL- have been synthesized using amino acid racemase and tryptophan synthetase are coupling catalysed
Propylhomoserin.The process route that enzyme process prepares DL-cysteine is as follows：
Technical solution provided by the invention solves the problems, such as following two：One, a kind of coupling catalysed preparation of multienzyme is provided
The technique of DL-cysteine, the technique is environmentally protective, high catalytic efficiency, eliminates intermediate product separation and Extraction process, and existing
Technology, which is compared, has stronger competitiveness；Two, solve substrate serine inexpensively carrys out source problem, and glycine and formaldehyde are all honest and clean
The raw material of industry that valence is easy to get significantly reduces the production cost of serine.
Compared with the prior art, the present invention has the following advantages：
(1) present invention uses the coupling catalysed preparation DL-cysteine of multienzyme, and reaction condition is mild, environmentally friendly, meets
The development trend of Modern Green chemical industry；
(2) enzyme law catalysis stereoselectivity is strong, high catalytic efficiency, D-Thr aldolase synthetic product D-Ser process
In, the molar yield of glycine is up to 98% or more；Amino acid racemase and tryptophan synthetase dual-enzyme coupling synthesize half Guangs of DL-
During propylhomoserin, 90% or more the molar yield of serine；
(3) raw material is cheap and easy to get, and glycine and formaldehyde are simplest industrial chemicals, greatly reduce DL-cysteine
Production cost, with good economic efficiency and social benefit；
(4) present invention process flow is simple, eliminates intermediate product separation and Extraction process, is suitble to industrialized production.
Four, specific implementation mode
Following embodiment is only used for that the present invention is specifically described, but protection scope of the present invention is not intended to be limited to
Following embodiment.
Embodiment one
1. taking the Xanthomonas campestris wet thallus 10g with D-Thr aldolase activity, it is added in 1000mL conversion fluids, turns
Change glycine containing 50g/L and 0.05g/L phosphopyridoxal pyridoxal phosphates in liquid, stream plus 100g/L formalin 200mL, controls reaction system
Middle formaldehyde final concentration is not higher than 5g/L, while utilizing 6.0, the 20 DEG C of oscillations of pH of 5mol/L sodium hydrate aqueous solutions control reaction solution
10h is reacted, efficient liquid phase detects D-Ser concentration 57.7g/L in reaction solution, and glycine molar yield 99% stops anti-
It answers.
2. taking 1000mL D-Ser conversion fluids, 4000r/min centrifuges 15min and removes somatic cells, is added in supernatant
NaHS 52.8g, control reaction solution pH 7.0, is added the pseudomonas putida wet thallus 5g with amino acid racemase activity
With with the active Escherichia coli wet thallus 10g of tryptophan synthetase, 30 DEG C of oscillating reactions 12h, efficient liquid phase detects reaction solution
Middle DL-cysteine concentration 59.8g/L, serine molar yield 90% stop reaction.
3. DL-cysteine conversion fluid 4000r/min centrifugations 15min is removed somatic cells, supernatant 6mol/L salt
Acid adjusts pH 1.5, heating removal H2S, decolorizing with activated carbon filter, and filtrate is with concentrated ammonia liquor tune pH5.0, by half Guangs of DL- in filtrate
Propylhomoserin blowing air aoxidizes, and white precipitate, vacuum filtration is precipitated, and 56.8g DL- cystine crude products are dried to obtain in the washing of 80% ethyl alcohol,
53.6g DL- cystine fine work, specific rotation are obtained after refined(c=2,1mol/L hydrochloric acid), DL- cystine fine work is through electricity
DL-cysteine is made in solution reduction.
Embodiment two
1. taking the Xanthomonas campestris wet thallus 15g with D-Thr aldolase activity, it is added in 1000mL conversion fluids, turns
Change glycine containing 80g/L and 0.1g/L phosphopyridoxal pyridoxal phosphates in liquid, stream plus 200g/L formalin 160mL, controls reaction system
Middle formaldehyde final concentration is not higher than 5g/L, while utilizing 7.0, the 30 DEG C of oscillations of pH of 5mol/L sodium hydrate aqueous solutions control reaction solution
8h is reacted, efficient liquid phase detects D-Ser concentration 95.6g/L in reaction solution, and glycine molar yield 99% stops reaction.
2. taking 1000mL D-Ser conversion fluids, 4000r/min centrifuges 15min and removes somatic cells, is added in supernatant
NaHS 87.4g, control reaction solution pH 8.5, is added the pseudomonas putida wet thallus with amino acid racemase activity
10g and with tryptophan synthetase active Escherichia coli wet thallus 15g, 37 DEG C of oscillating reactions 10h, efficient liquid phase detection reaction
DL-cysteine concentration 100.3g/L in liquid, serine molar yield 91% stop reaction.
3. DL-cysteine conversion fluid 4000r/min centrifugations 15min is removed somatic cells, supernatant 6mol/L salt
Acid adjusts pH 1.5, heating removal H2S, decolorizing with activated carbon filter, and filtrate is with concentrated ammonia liquor tune pH5.0, by half Guangs of DL- in filtrate
Propylhomoserin blowing air aoxidizes, and white precipitate, vacuum filtration is precipitated, and 94.2g DL- cystine crude products are dried to obtain in the washing of 80% ethyl alcohol,
89.5g DL- cystine fine work, specific rotation are obtained after refined(c=2,1mol/L hydrochloric acid), DL- cystine fine work is through electricity
DL-cysteine is made in solution reduction.
Embodiment three
1. taking the Xanthomonas campestris wet thallus 20g with D-Thr aldolase activity, it is added in 1000mL conversion fluids, turns
Change glycine containing 100g/L and 0.2g/L phosphopyridoxal pyridoxal phosphates in liquid, stream plus 300g/L formalin 134mL, controls reaction system
Middle formaldehyde final concentration is not higher than 5g/L, while utilizing 8.0, the 35 DEG C of oscillations of pH of 5mol/L sodium hydrate aqueous solutions control reaction solution
12h is reacted, efficient liquid phase detects D-Ser concentration 122.3g/L in reaction solution, and glycine molar yield 99% stops anti-
It answers.
2. taking 1000mL D-Ser conversion fluids, 4000r/min centrifuges 15min and removes somatic cells, is added in supernatant
NaHS 111.8g, control reaction solution pH 9.0, is added the pseudomonas putida wet thallus with amino acid racemase activity
10g and with tryptophan synthetase active Escherichia coli wet thallus 20g, 40 DEG C of oscillating reactions 15h, efficient liquid phase detection reaction
DL-cysteine concentration 126.8g/L in liquid, serine molar yield 90% stop reaction.
3. DL-cysteine conversion fluid 4000r/min centrifugations 15min is removed somatic cells, supernatant 6mol/L salt
Acid adjusts pH 1.5, heating removal H2S, decolorizing with activated carbon filter, and filtrate is with concentrated ammonia liquor tune pH5.0, by half Guangs of DL- in filtrate
Propylhomoserin blowing air aoxidizes, and white precipitate, vacuum filtration is precipitated, and the washing of 80% ethyl alcohol dries to obtain 120g DL- cystine crude products, essence
110.9g DL- cystine fine work, specific rotation are obtained after system(c=2,1mol/L hydrochloric acid), DL- cystines fine work is through electrolysis
DL-cysteine is made in reduction.
Example IV
1. taking the Xanthomonas campestris wet thallus 20g with D-Thr aldolase activity, it is added in 1000mL conversion fluids, turns
Change glycine containing 120g/L and 0.2g/L phosphopyridoxal pyridoxal phosphates in liquid, stream plus 300g/L formalin 160mL, controls reaction system
Middle formaldehyde final concentration is not higher than 5g/L, while utilizing 9.0, the 40 DEG C of oscillations of pH of 5mol/L sodium hydrate aqueous solutions control reaction solution
15h is reacted, efficient liquid phase detects D-Ser concentration 143.4g/L in reaction solution, and glycine molar yield 99% stops anti-
It answers.
2. taking 1000mL D-Ser conversion fluids, 4000r/min centrifuges 15min and removes somatic cells, is added in supernatant
NaHS 131g, control reaction solution pH 10.0, is added the pseudomonas putida wet thallus with amino acid racemase activity
10g and with tryptophan synthetase active Escherichia coli wet thallus 20g, 50 DEG C of oscillating reactions 15h, efficient liquid phase detection reaction
DL-cysteine concentration 150.4g/L in liquid, serine molar yield 91% stop reaction.
3. DL-cysteine conversion fluid 4000r/min centrifugations 15min is removed somatic cells, supernatant 6mol/L salt
Acid adjusts pH 1.5, heating removal H2S, decolorizing with activated carbon filter, and filtrate is with concentrated ammonia liquor tune pH5.0, by half Guangs of DL- in filtrate
Propylhomoserin blowing air aoxidizes, and white precipitate, vacuum filtration is precipitated, and 141.4g DL- cystine crude products are dried to obtain in the washing of 80% ethyl alcohol,
131.5g DL- cystine fine work, specific rotation are obtained after refined(c=2,1mol/L hydrochloric acid), DL- cystine fine work is through electricity
DL-cysteine is made in solution reduction.
Embodiment five
1. taking the Xanthomonas campestris wet thallus 30g with D-Thr aldolase activity, it is added in 1000mL conversion fluids, turns
Change glycine containing 150g/L and 0.3g/L phosphopyridoxal pyridoxal phosphates in liquid, stream plus 370g/L formalin 162mL, controls reaction system
Middle formaldehyde final concentration is not higher than 5g/L, while utilizing 7.5, the 35 DEG C of oscillations of pH of 5mol/L sodium hydrate aqueous solutions control reaction solution
20h is reacted, efficient liquid phase detects D-Ser concentration 179g/L in reaction solution, and glycine molar yield 99% stops reaction.
2. taking 1000mL D-Ser conversion fluids, 4000r/min centrifuges 15min and removes somatic cells, is added in supernatant
NaHS 163.6g, control reaction solution pH 8.2, is added the pseudomonas putida wet thallus with amino acid racemase activity
15g and with tryptophan synthetase active Escherichia coli wet thallus 30g, 35 DEG C of oscillating reactions 20h, efficient liquid phase detection reaction
DL-cysteine concentration 185.6g/L in liquid, serine molar yield 90% stop reaction.
3. DL-cysteine conversion fluid 4000r/min centrifugations 15min is removed somatic cells, supernatant 6mol/L salt
Acid adjusts pH 1.5, heating removal H2S, decolorizing with activated carbon filter, and filtrate is with concentrated ammonia liquor tune pH5.0, by half Guangs of DL- in filtrate
Propylhomoserin blowing air aoxidizes, and white precipitate, vacuum filtration is precipitated, and 174.5g DL- cystine crude products are dried to obtain in the washing of 80% ethyl alcohol,
162.3g DL- cystine fine work, specific rotation are obtained after refined(c=2,1mol/L hydrochloric acid), DL- cystine fine work is through electricity
DL-cysteine is made in solution reduction.
Embodiment six
1. taking the Xanthomonas campestris wet thallus 40g with D-Thr aldolase activity, it is added in 1000mL conversion fluids, turns
Change glycine containing 180g/L and 0.5g/L phosphopyridoxal pyridoxal phosphates in liquid, stream plus 370g/L formalin 195mL, controls reaction system
Middle formaldehyde final concentration is not higher than 5g/L, while utilizing 7.0, the 37 DEG C of oscillations of pH of 5mol/L sodium hydrate aqueous solutions control reaction solution
28h is reacted, efficient liquid phase detects D-Ser concentration 209g/L in reaction solution, and glycine molar yield 99% stops reaction.
2. taking 1000mL D-Ser conversion fluids, 4000r/min centrifuges 15min and removes somatic cells, is added in supernatant
NaHS 191g, control reaction solution pH 8.2, is added the pseudomonas putida wet thallus 20g with amino acid racemase activity
With with the active Escherichia coli wet thallus 35g of tryptophan synthetase, 37 DEG C of oscillating reactions 30h, efficient liquid phase detects reaction solution
Middle DL-cysteine concentration 217g/L, serine molar yield 90% stop reaction.
3. DL-cysteine conversion fluid 4000r/min centrifugations 15min is removed somatic cells, supernatant 6mol/L salt
Acid adjusts pH 1.5, heating removal H2S, decolorizing with activated carbon filter, and filtrate is with concentrated ammonia liquor tune pH5.0, by half Guangs of DL- in filtrate
Propylhomoserin blowing air aoxidizes, and white precipitate, vacuum filtration is precipitated, and the washing of 80% ethyl alcohol dries to obtain 203g DL- cystine crude products, essence
189g DL- cystine fine work, specific rotation are obtained after system (c=2,1mol/L hydrochloric acid), DL- cystines fine work are gone back through electrolysis
The obtained DL-cysteine of original.
Claims (1)
1. a kind of method that enzymatic conversion method prepares DL-cysteine, feature are made of following steps：
(1) by bacterial strain of the Xanthomonas campestris source with D-Thr aldolase activity, pseudomonas putida source with amino acid
There is bacterial strain, the Escherichia coli of Racemase activity the active bacterial strain of tryptophan synthetase to cultivate in the medium respectively, point
Not Chan Sheng high activity D-Thr aldolase, amino acid racemase, tryptophan synthetase；Culture medium carbon source using glucose,
Maltose, sucrose and/or lactose, total carbon source mass concentration is 1~20g/L in culture medium；Nitrogen source using beef extract, yeast extract,
Corn steep liquor, peptone and/or soya-bean cake hydrolyzate, total nitrogen source mass concentration is 1~20g/L in culture medium；
(2) using the glycine of 50~180g/L as substrate, being added has the somatic cells of D-Thr aldolase activity or enzyme thick
Extract, the phosphopyridoxal pyridoxal phosphate of 0.05~0.5g/L, 20~40 DEG C, stream adds the formalin of 100~370g/L, uses sodium hydroxide
Aqueous solution controls pH 6~9, and enzymatic converts to obtain D-Ser；
(3) D-Ser conversion fluid removes somatic cells through centrifugation, and NaHS is added, and ammonia is added in 7~10,30~50 DEG C of pH
Base acid racemase somatic cells or crude enzyme liquid, tryptophan synthetase somatic cells or crude enzyme liquid, dual-enzyme coupling catalyze and synthesize DL- half
Cystine；
(4) by the DL-cysteine blowing air of generation or dropwise addition hydrogen peroxide oxidation, the isolated DL- Guangs ammonia of isoelectric point crystallizing method
Acid, then DL-cysteine is made through electroreduction.
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