DD282918A5 - Enzymatisches verfahren zur herstellung von peptiden, insbesondere dipeptiden und vorrichtung dafuer - Google Patents

Enzymatisches verfahren zur herstellung von peptiden, insbesondere dipeptiden und vorrichtung dafuer Download PDF

Info

Publication number: DD282918A5
Authority: DD; German Democratic Republic
Prior art keywords: amino acid; protected; reaction; peptide; enzyme
Prior art date: 1987-10-01

Application number

DD88320269A

Other languages

German (de)

English (en)

Inventor

Hans-Juergen Schuetz

Christian Wandrey

Original Assignee

Kernforschungsanlage Juelich,De

Priority date (The priority date 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 date listed.)

1987-10-01

Filing date

1988-09-29

Publication date

1990-09-26

1988-09-29 Application filed by Kernforschungsanlage Juelich,De filed Critical Kernforschungsanlage Juelich,De

1990-09-26 Publication of DD282918A5 publication Critical patent/DD282918A5/de

Links

108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 30
108010016626 Dipeptides Proteins 0.000 title claims abstract description 22
238000000034 method Methods 0.000 title claims abstract description 19
230000002255 enzymatic effect Effects 0.000 title claims abstract description 12
102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 10
238000002360 preparation method Methods 0.000 title claims abstract description 9
230000008569 process Effects 0.000 title claims abstract description 6
108090000790 Enzymes Proteins 0.000 claims abstract description 32
102000004190 Enzymes Human genes 0.000 claims abstract description 32
238000006243 chemical reaction Methods 0.000 claims abstract description 29
150000001413 amino acids Chemical class 0.000 claims abstract description 17
-1 N-protected amino Chemical group 0.000 claims abstract description 15
239000012528 membrane Substances 0.000 claims abstract description 13
125000006239 protecting group Chemical group 0.000 claims abstract description 13
150000002148 esters Chemical class 0.000 claims abstract description 11
239000011541 reaction mixture Substances 0.000 claims abstract description 11
230000015572 biosynthetic process Effects 0.000 claims abstract description 10
108010073038 Penicillin Amidase Proteins 0.000 claims abstract description 8
238000001179 sorption measurement Methods 0.000 claims abstract description 8
125000005907 alkyl ester group Chemical group 0.000 claims abstract description 6
239000008346 aqueous phase Substances 0.000 claims abstract description 5
230000002209 hydrophobic effect Effects 0.000 claims abstract description 5
238000010647 peptide synthesis reaction Methods 0.000 claims abstract description 5
239000007864 aqueous solution Substances 0.000 claims abstract description 4
238000006911 enzymatic reaction Methods 0.000 claims abstract description 4
239000002904 solvent Substances 0.000 claims abstract description 4
102000005367 Carboxypeptidases Human genes 0.000 claims abstract description 3
108010006303 Carboxypeptidases Proteins 0.000 claims abstract description 3
102000035195 Peptidases Human genes 0.000 claims abstract description 3
108091005804 Peptidases Proteins 0.000 claims abstract description 3
102000012479 Serine Proteases Human genes 0.000 claims abstract description 3
108010022999 Serine Proteases Proteins 0.000 claims abstract description 3
239000002253 acid Substances 0.000 claims abstract description 3
238000010511 deprotection reaction Methods 0.000 claims abstract description 3
230000007717 exclusion Effects 0.000 claims abstract description 3
235000019833 protease Nutrition 0.000 claims abstract description 3
235000001014 amino acid Nutrition 0.000 claims description 27
229940024606 amino acid Drugs 0.000 claims description 27
QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims description 10
235000004279 alanine Nutrition 0.000 claims description 10
229920001429 chelating resin Polymers 0.000 claims description 8
238000003776 cleavage reaction Methods 0.000 claims description 7
230000007017 scission Effects 0.000 claims description 7
230000020176 deacylation Effects 0.000 claims description 5
238000005947 deacylation reaction Methods 0.000 claims description 5
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 4
238000000926 separation method Methods 0.000 claims description 4
230000000717 retained effect Effects 0.000 claims description 3
MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 claims description 2
239000004475 Arginine Substances 0.000 claims description 2
239000004471 Glycine Substances 0.000 claims description 2
ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims description 2
AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims description 2
ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 2
FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 2
KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims description 2
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 2
MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 2
KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims description 2
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 2
229960000310 isoleucine Drugs 0.000 claims description 2
AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims description 2
229930182817 methionine Natural products 0.000 claims description 2
239000004474 valine Substances 0.000 claims description 2
238000009825 accumulation Methods 0.000 claims 1
239000003480 eluent Substances 0.000 claims 1
NLKUJNGEGZDXGO-XVKPBYJWSA-N Tyr-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 NLKUJNGEGZDXGO-XVKPBYJWSA-N 0.000 abstract description 3
238000004519 manufacturing process Methods 0.000 abstract description 2
235000016236 parenteral nutrition Nutrition 0.000 abstract description 2
150000001875 compounds Chemical class 0.000 abstract 1
230000014759 maintenance of location Effects 0.000 abstract 1
235000016709 nutrition Nutrition 0.000 abstract 1
230000035764 nutrition Effects 0.000 abstract 1
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 4
108010038807 Oligopeptides Proteins 0.000 description 4
102000015636 Oligopeptides Human genes 0.000 description 4
WLJVXDMOQOGPHL-UHFFFAOYSA-N phenylacetic acid Chemical compound OC(=O)CC1=CC=CC=C1 WLJVXDMOQOGPHL-UHFFFAOYSA-N 0.000 description 4
239000000243 solution Substances 0.000 description 4
OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
230000009849 deactivation Effects 0.000 description 3
239000007788 liquid Substances 0.000 description 3
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
238000002425 crystallisation Methods 0.000 description 2
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238000010828 elution Methods 0.000 description 2
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238000006460 hydrolysis reaction Methods 0.000 description 2
239000000543 intermediate Substances 0.000 description 2
230000000144 pharmacologic effect Effects 0.000 description 2
239000012071 phase Substances 0.000 description 2
229960003424 phenylacetic acid Drugs 0.000 description 2
239000003279 phenylacetic acid Substances 0.000 description 2
239000000758 substrate Substances 0.000 description 2
238000003786 synthesis reaction Methods 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
238000010626 work up procedure Methods 0.000 description 2
102000005572 Cathepsin A Human genes 0.000 description 1
108010059081 Cathepsin A Proteins 0.000 description 1
108010093096 Immobilized Enzymes Proteins 0.000 description 1
GSYTVXOARWSQSV-BYPYZUCNSA-N L-methioninamide Chemical compound CSCC[C@H](N)C(N)=O GSYTVXOARWSQSV-BYPYZUCNSA-N 0.000 description 1
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 description 1
JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
JXNRXNCCROJZFB-RYUDHWBXSA-N Tyr-Arg Chemical compound NC(=N)NCCC[C@@H](C(O)=O)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 JXNRXNCCROJZFB-RYUDHWBXSA-N 0.000 description 1
239000006096 absorbing agent Substances 0.000 description 1
125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 description 1
230000009471 action Effects 0.000 description 1
125000001931 aliphatic group Chemical group 0.000 description 1
125000000217 alkyl group Chemical group 0.000 description 1
150000001408 amides Chemical class 0.000 description 1
125000003236 benzoyl group Chemical group [H]C1=C([H])C([H])=C(C([H])=C1[H])C(*)=O 0.000 description 1
125000004432 carbon atom Chemical group C* 0.000 description 1
239000000969 carrier Substances 0.000 description 1
230000008859 change Effects 0.000 description 1
238000001311 chemical methods and process Methods 0.000 description 1
239000012295 chemical reaction liquid Substances 0.000 description 1
238000013375 chromatographic separation Methods 0.000 description 1
238000001514 detection method Methods 0.000 description 1
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125000003700 epoxy group Chemical group 0.000 description 1
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230000006872 improvement Effects 0.000 description 1
239000003978 infusion fluid Substances 0.000 description 1
108010053037 kyotorphin Proteins 0.000 description 1
230000003287 optical effect Effects 0.000 description 1
239000000813 peptide hormone Substances 0.000 description 1
239000008177 pharmaceutical agent Substances 0.000 description 1
229920000642 polymer Polymers 0.000 description 1
235000018102 proteins Nutrition 0.000 description 1
102000004169 proteins and genes Human genes 0.000 description 1
108090000623 proteins and genes Proteins 0.000 description 1
239000007858 starting material Substances 0.000 description 1
238000003860 storage Methods 0.000 description 1
230000007306 turnover Effects 0.000 description 1
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/20—Partition-, reverse-phase or hydrophobic interaction chromatography
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/02—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length in solution
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- 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
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02P—CLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
- Y02P20/00—Technologies relating to chemical industry
- Y02P20/50—Improvements relating to the production of bulk chemicals
- Y02P20/55—Design of synthesis routes, e.g. reducing the use of auxiliary or protecting groups
- 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
- Y10S435/803—Physical recovery methods, e.g. chromatography, grinding
- 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
- Y10S435/813—Continuous fermentation

Landscapes

Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Genetics & Genomics (AREA)
Biochemistry (AREA)
Biophysics (AREA)
General Health & Medical Sciences (AREA)
Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Molecular Biology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Life Sciences & Earth Sciences (AREA)
Analytical Chemistry (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)

DD88320269A 1987-10-01 1988-09-29 Enzymatisches verfahren zur herstellung von peptiden, insbesondere dipeptiden und vorrichtung dafuer DD282918A5 (de)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
DE19873733198 DE3733198A1 (de)	1987-10-01	1987-10-01	Enzymatisches verfahren zur herstellung von dipeptiden

Publications (1)

Publication Number	Publication Date
DD282918A5 true DD282918A5 (de)	1990-09-26

Family

ID=6337394

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
DD88320269A DD282918A5 (de)	1987-10-01	1988-09-29	Enzymatisches verfahren zur herstellung von peptiden, insbesondere dipeptiden und vorrichtung dafuer

Country Status (6)

Country	Link
US (1)	US5057415A (fr)
EP (1)	EP0309983A3 (fr)
JP (1)	JPH01222795A (fr)
DD (1)	DD282918A5 (fr)
DE (1)	DE3733198A1 (fr)
DK (1)	DK549688A (fr)

Families Citing this family (16)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
DE4014564C1 (fr) *	1990-05-07	1991-07-18	Forschungszentrum Juelich Gmbh, 5170 Juelich, De
DE4101895C1 (fr) *	1991-01-23	1991-12-05	Forschungszentrum Juelich Gmbh, 5170 Juelich, De
US5874532A (en) *	1997-01-08	1999-02-23	Nexstar Pharmaceuticals, Inc.	Method for solution phase synthesis of oligonucleotides and peptides
JPH11171895A (ja) *	1997-12-11	1999-06-29	Ajinomoto Co Inc	アスパルテームとアスパルテーム誘導体の分離精製方法
WO2002094855A2 (fr) *	2001-05-23	2002-11-28	Diversa Corporation	Methode de synthese peptidique
EP2681326A4 (fr) *	2011-02-28	2016-11-09	Politechnic Inst Univ New York	Préparation de mélanges peptidiques par catalyse des protéases conçus pour donner des propriétés physiques et biologiques utiles
TW202446781A (zh)	2011-12-28	2024-12-01	日商中外製藥股份有限公司	胜肽化合物之製造方法
EP4166664A1 (fr)	2015-03-13	2023-04-19	Chugai Seiyaku Kabushiki Kaisha	Aminoacyl-arnt synthétase modifiée et utilisation correspondante
JP7187323B2 (ja) *	2017-01-31	2022-12-12	中外製薬株式会社	無細胞翻訳系におけるペプチドの合成方法
KR20250007021A (ko)	2017-06-09	2025-01-13	추가이 세이야쿠 가부시키가이샤	N-치환 아미노산을 포함하는 펩타이드의 합성 방법
WO2019117274A1 (fr)	2017-12-15	2019-06-20	中外製薬株式会社	Procédé de fabrication de peptide, et procédé de traitement de base
EP3878836B1 (fr)	2018-11-07	2025-07-23	Chugai Seiyaku Kabushiki Kaisha	Procédé de production d'un dérivé de sérine o-substitué
WO2020111238A1 (fr)	2018-11-30	2020-06-04	中外製薬株式会社	Procédé de déprotection et procédé d'élimination de résine dans une réaction en phase solide d'un composé peptidique ou d'un composé amide, et procédé de production d'un composé peptidique
EP3939962A4 (fr)	2019-03-15	2022-12-28	Chugai Seiyaku Kabushiki Kaisha	Procédé de préparation d'un dérivé d'acide aminé aromatique
BR112022007535A2 (pt)	2019-11-07	2022-07-12	Chugai Pharmaceutical Co Ltd	Composto peptídico cíclico tendo ação inibitória de kras
DE102021108406A1 (de) *	2021-04-01	2022-10-06	Jacobs University Bremen Ggmbh	Vorrichtung und Verfahren zum Abtrennen von in einer Trägerflüssigkeit aufgenommenen Proteinen

Family Cites Families (4)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
FI70597C (fi) *	1979-04-06	1986-09-24	Carlsberg Biotechnology Ltd	Foerfarande foer enzymatisk framstaellning av peptider
DE2930087A1 (de) *	1979-07-25	1981-02-26	Biotechnolog Forschung Gmbh	Verfahren zur kontinuierlichen enzymatischen umwandlung von wasserloeslichen alpha -ketocarbonsaeuren in die entsprechenden alpha -hydroxycarbonsaeuren
DE2930070A1 (de) *	1979-07-25	1981-02-19	Biotechnolog Forschung Gmbh	Verfahren zur kontinuierlichen enzymatischen umwandlung von wasserloeslichen alpha -ketocarbonsaeuren in die entsprechenden aminosaeuren
DK72587D0 (da) *	1987-02-13	1987-02-13	Carlsberg Biotechnology Ltd	Fremgangsmaade til enzymatisk fremstilling af dipeptider

1987
- 1987-10-01 DE DE19873733198 patent/DE3733198A1/de not_active Withdrawn
1988
- 1988-09-27 EP EP19880115873 patent/EP0309983A3/fr not_active Withdrawn
- 1988-09-29 JP JP63242646A patent/JPH01222795A/ja active Pending
- 1988-09-29 DD DD88320269A patent/DD282918A5/de not_active IP Right Cessation
- 1988-09-30 US US07/251,176 patent/US5057415A/en not_active Expired - Fee Related
- 1988-09-30 DK DK549688A patent/DK549688A/da not_active Application Discontinuation

Also Published As

Publication number	Publication date
US5057415A (en)	1991-10-15
JPH01222795A (ja)	1989-09-06
EP0309983A3 (fr)	1991-03-27
EP0309983A2 (fr)	1989-04-05
DK549688A (da)	1989-04-02
DK549688D0 (da)	1988-09-30
DE3733198A1 (de)	1989-04-13

Legal Events

Date	Code	Title	Description
1995-06-08	ENJ	Ceased due to non-payment of renewal fee

Publication	Publication Date	Title
DD282918A5 (de)	1990-09-26	Enzymatisches verfahren zur herstellung von peptiden, insbesondere dipeptiden und vorrichtung dafuer
EP0087750B1 (fr)	1985-06-19	Préparation d'aminoacides contenant des restes glutaminiques
DE3012693C2 (fr)	1990-04-26
DE3884976T2 (de)	1994-02-17	Verfahren zur enzymatischen Herstellung von Dipeptiden.
SU1705302A1 (ru)	1992-01-15	Способ препаративной экспрессии генов в бесклеточной системе сопр женной транскрипции/трансл ции
DE3789309T2 (de)	1994-10-06	Enzymatische membran, verfahren zur herstellung und trennung von peptiden.
DE3887246T2 (de)	1994-07-28	Verfahren zur Herstellung von Glutamin-Derivaten.
DE69010405T2 (de)	1994-10-20	Verfahren zur Herstellung von R(+)-Aminocarnitin und S(-)-Aminocarnitin.
Könnecke et al.	1981	Peptide synthesis by means of immobilized enzymes: I. Immobilized α-chymotrypsin
DE3781555T2 (de)	1993-02-25	Verfahren zur herstellung einer zwei diastereoisomerische n-acylaminosaeureester enthaltenden diastereoisomerischen mischung.
Toda et al.	1988	A new chiral host compound 10, 10′-dihyrroxy-9, 9′-biphenanthryl. Optical resolution of propionic acid derivatives, butyric acid derivatives, and 4-hydroxycyclopent-2-en-1-one derivatives by complexation
DE3203292C2 (fr)	1990-01-11
DE10220740A1 (de)	2003-11-27	Verfahren zur enzymatischen Herstellung enantiomerenangereicherter beta-Aminosäuren
JP2001011034A (ja)	2001-01-16	光学活性アミノ酸と光学活性アミノ酸アミドの分離回収方法
DE69736561T2 (de)	2007-08-23	Acyltransfer mit einem stabilisierten übergangskomplex unter verwendung eines katalysators mit einer katalytischen imidazolfunktion (z.b. histidin)
FR2496660A1 (fr)	1982-06-25	Procede de preparation de n-acylcarnosine
DE60119491T2 (de)	2006-11-16	Verfahren zur herstellung von acetylamidiniophenylalanyl-cyclohexylglycyl-pyridylalaninamiden
DE10320211A1 (de)	2004-02-12	Verfahren zur enzymatischen Herstellung enantiomerenangereicherter β-Aminosäuren
DE3318932C1 (de)	1984-06-07	Verfahren zur Gewinnung von reinem L-Leucin
CN110407913A (zh)	2019-11-05	一种丙谷二肽的分离提纯方法
JP2001328970A (ja)	2001-11-27	光学活性α−アミノ酸及び光学活性α−アミノ酸アミドの製造方法
AU2003241004B2 (en)	2008-07-31	Continuous process for the cyanation of hydrogenated beta-ketoesters
DE3741515C2 (fr)	1989-12-07
DE2008842A1 (de)	1970-11-05	Verfahren und Vorrichtung zur kontinuierlichen Durchführung von Enzymreaktionen
DE68906086T2 (de)	1993-09-09	Von spergualin abgeleitete verbindungen, verfahren zu ihrer herstellung und ihre verwendung.