Highly efficient synthesis of ampicillin in an "aqueous solution-precipitate" system: Repetitive addition of substrates in a semicontinuous process
The synthesis of ampicillin catalyzed by Escherichia coli penicillin acylase was optimized in an aqueous system with partially dissolved antibiotic nucleus 6‐aminopenicillanic acid (6‐APA). The yields of both 6‐APA and acyl donor could be improved by repetitively adding substrates to the reaction, a...
Saved in:
Published in: | Biotechnology and bioengineering Vol. 73; no. 5; pp. 426 - 430 |
---|---|
Main Authors: | , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
New York
John Wiley & Sons, Inc
05-06-2001
Wiley |
Subjects: | |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Abstract | The synthesis of ampicillin catalyzed by Escherichia coli penicillin acylase was optimized in an aqueous system with partially dissolved antibiotic nucleus 6‐aminopenicillanic acid (6‐APA). The yields of both 6‐APA and acyl donor could be improved by repetitively adding substrates to the reaction, allowing the concentration of 6‐APA to remain saturated throughout. In this reaction concept, with four subsequent additions of substrates, 97% conversion of 6‐APA and 72% of D‐(−)‐phenylglycine methyl ester (D‐PGM) to ampicillin was achieved. The synthetic potential of this concept was estimated using a mathematical model which showed that by increasing the amount of added substrates a nearly quantitative conversion of 6‐APA and 85% conversion of acyl donor into ampicillin could be achieved . © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 73: 426–430, 2001. |
---|---|
AbstractList | The synthesis of ampicillin catalyzed by Escherichia coli penicillin acylase was optimized in an aqueous system with partially dissolved antibiotic nucleus 6-aminopenicillanic acid (6-APA). The yields of both 6-APA and acyl donor could be improved by repetitively adding substrates to the reaction, allowing the concentration of 6-APA to remain saturated throughout. In this reaction concept, with four subsequent additions of substrates, 97% conversion of 6-APA and 72% of D-(-)-phenylglycine methyl ester (D-PGM) to ampicillin was achieved. The synthetic potential of this concept was estimated using a mathematical model which showed that by increasing the amount of added substrates a nearly quantitative conversion of 6-APA and 85% conversion of acyl donor into ampicillin could be achieved. The synthesis of ampicillin catalyzed by Escherichia coli penicillin acylase was optimized in an aqueous system with partially dissolved antibiotic nucleus 6‐aminopenicillanic acid (6‐APA). The yields of both 6‐APA and acyl donor could be improved by repetitively adding substrates to the reaction, allowing the concentration of 6‐APA to remain saturated throughout. In this reaction concept, with four subsequent additions of substrates, 97% conversion of 6‐APA and 72% of D‐(−)‐phenylglycine methyl ester (D‐PGM) to ampicillin was achieved. The synthetic potential of this concept was estimated using a mathematical model which showed that by increasing the amount of added substrates a nearly quantitative conversion of 6‐APA and 85% conversion of acyl donor into ampicillin could be achieved . © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 73: 426–430, 2001. The synthesis of ampicillin catalyzed by Escherichia coli penicillin acylase was optimized in an aqueous system with partially dissolved antibiotic nucleus 6‐aminopenicillanic acid (6‐APA). The yields of both 6‐APA and acyl donor could be improved by repetitively adding substrates to the reaction, allowing the concentration of 6‐APA to remain saturated throughout. In this reaction concept, with four subsequent additions of substrates, 97% conversion of 6‐APA and 72% of D ‐(−)‐phenylglycine methyl ester (D‐PGM) to ampicillin was achieved. The synthetic potential of this concept was estimated using a mathematical model which showed that by increasing the amount of added substrates a nearly quantitative conversion of 6‐APA and 85% conversion of acyl donor into ampicillin could be achieved . © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 73: 426–430, 2001. |
Author | Sheldon, Roger A. van Langen, Luuk M. Švedas, Vytas K. de Vroom, Erik van Rantwijk, Fred Youshko, Maxim I. |
Author_xml | – sequence: 1 givenname: Maxim I. surname: Youshko fullname: Youshko, Maxim I. organization: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119899 Moscow, Russia; fax: +7 095 9393181 – sequence: 2 givenname: Luuk M. surname: van Langen fullname: van Langen, Luuk M. organization: Laboratory of Organic Chemistry and Catalysis, Delft University of Technology, Delft, The Netherlands – sequence: 3 givenname: Erik surname: de Vroom fullname: de Vroom, Erik organization: DSM Anti-Infectives, Delft, The Netherlands – sequence: 4 givenname: Fred surname: van Rantwijk fullname: van Rantwijk, Fred organization: Laboratory of Organic Chemistry and Catalysis, Delft University of Technology, Delft, The Netherlands – sequence: 5 givenname: Roger A. surname: Sheldon fullname: Sheldon, Roger A. organization: Laboratory of Organic Chemistry and Catalysis, Delft University of Technology, Delft, The Netherlands – sequence: 6 givenname: Vytas K. surname: Švedas fullname: Švedas, Vytas K. email: Vytas@enzyme.genebee.msu.su organization: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119899 Moscow, Russia; fax: +7 095 9393181 |
BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1102374$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/11320513$$D View this record in MEDLINE/PubMed |
BookMark | eNqFkduK1TAUhoOMOHtGwSeQMoh4U11pmh7mTkedA4OKjAhzE9J0xYm2ae1K1f0cvrCpu6g3IgRy4Mv_s_gO2J4fPDJ2n8MTDpA9bVyIh7K4xTYc6jKFrIY9tgGAIhWyzvbZAdGneC2rorjD9jkXGUguNuzHmft4020TtNYZhz4ktPXhBslRMthE92N87jrnk7i0T470lxmHmRIaujm4wafjhMaNLuiAR_EzBeyPk3c4YnDBfcVEt61bwCWO5obCFEn6FZcQ9s4MPjg_L5njNBgkustuW90R3lv3Q_b-1curk7P08s3p-cmzy9TkXBZp3WBrZQ4lSGFbIQFkUYHMTWWRZ01VSV0VedNKK5q6FFiAFRbyXDd5CQIzccge7XJjb5yKguodGew67ZcRVQkV1BnAf0FecRnL8wg-3oFmGogmtGqcXK-nreKgFlMqmlKLqYg-WDPnpsf2D7iqicDDFdBkdGcn7Y2jvzjIRLlUpjvsm-tw-88-9fz8au1deRdNff_N6-mzKkpRSvXh9am6uH5xcV2_zVUhfgKgCLy7 |
CODEN | BIBIAU |
CitedBy_id | crossref_primary_10_1016_j_enzmictec_2006_03_041 crossref_primary_10_1007_s00253_006_0752_4 crossref_primary_10_55959_MSU0579_9384_2_2023_64_4_334_352 crossref_primary_10_1002_bit_22142 crossref_primary_10_1016_S1570_9639_02_00413_2 crossref_primary_10_1016_j_enzmictec_2004_04_021 crossref_primary_10_1016_j_enzmictec_2015_03_003 crossref_primary_10_1016_j_enzmictec_2006_10_014 crossref_primary_10_1016_S0958_1669_02_00336_1 crossref_primary_10_1002_adsc_200303023 crossref_primary_10_1016_j_procbio_2015_06_023 crossref_primary_10_1002_ejoc_200801204 crossref_primary_10_1007_s00253_013_4945_3 crossref_primary_10_1016_S0141_0229_03_00036_X crossref_primary_10_1016_j_molcatb_2006_01_029 crossref_primary_10_1002_bit_10863 crossref_primary_10_1007_s00449_011_0560_9 crossref_primary_10_1016_j_bioeng_2006_09_003 crossref_primary_10_1016_j_bioorg_2020_103765 crossref_primary_10_1080_10242420500292336 crossref_primary_10_3103_S0027131410030053 crossref_primary_10_1002_bit_10661 crossref_primary_10_1016_j_molcatb_2005_04_015 crossref_primary_10_1016_j_biotechadv_2005_05_003 crossref_primary_10_1016_j_molcatb_2007_04_003 crossref_primary_10_1002_bit_28214 crossref_primary_10_1007_BF02931061 crossref_primary_10_1016_j_chemolab_2007_09_006 crossref_primary_10_1016_S0032_9592_03_00031_1 crossref_primary_10_1016_S0166_1280_03_00231_8 crossref_primary_10_1007_s12257_011_0674_6 crossref_primary_10_1016_j_molcatb_2007_12_004 crossref_primary_10_1016_j_molcatb_2003_09_003 crossref_primary_10_1080_10242420601141762 crossref_primary_10_3389_fbioe_2022_936487 crossref_primary_10_1016_j_molcatb_2008_12_020 crossref_primary_10_1016_S0032_9592_02_00092_4 crossref_primary_10_1039_D0RE00272K crossref_primary_10_1016_j_jbiotec_2007_08_039 crossref_primary_10_1002_bit_22867 crossref_primary_10_3103_S0027131423040041 crossref_primary_10_1016_j_enzmictec_2010_07_010 crossref_primary_10_1002_chem_201804970 crossref_primary_10_1021_ie0614071 crossref_primary_10_1590_S1516_89132005000400003 crossref_primary_10_1016_j_catcom_2016_02_014 crossref_primary_10_1002_bit_10234 |
Cites_doi | 10.1016/S1381-1177(98)00044-7 10.1007/978-1-4684-3719-5_8 10.1007/BF01040031 10.1016/0141-0229(80)90070-8 10.1023/A:1002896621567 10.1016/S0141-0229(98)00053-2 10.1042/bj1150757 10.1016/S1381-1177(00)00091-6 10.1016/0005-2744(80)90145-X 10.1016/S0014-5793(99)00939-4 10.1016/S0141-0229(96)00032-4 10.1016/S0022-5193(89)80128-6 10.1515/bchm2.1984.365.2.1435 10.1021/op9700643 10.1016/0006-291X(82)91380-8 10.1016/1381-1177(95)00009-7 10.1016/S0141-0229(98)00140-9 10.1016/0141-0229(80)90103-9 |
ContentType | Journal Article |
Copyright | Copyright © 2001 John Wiley & Sons, Inc. 2001 INIST-CNRS Copyright 2001 John Wiley & Sons, Inc. |
Copyright_xml | – notice: Copyright © 2001 John Wiley & Sons, Inc. – notice: 2001 INIST-CNRS – notice: Copyright 2001 John Wiley & Sons, Inc. |
DBID | BSCLL IQODW CGR CUY CVF ECM EIF NPM AAYXX CITATION 7QO 8FD FR3 P64 7X8 |
DOI | 10.1002/bit.1076 |
DatabaseName | Istex Pascal-Francis Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Biotechnology Research Abstracts Technology Research Database Engineering Research Database Biotechnology and BioEngineering Abstracts MEDLINE - Academic |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Engineering Research Database Biotechnology Research Abstracts Technology Research Database Biotechnology and BioEngineering Abstracts MEDLINE - Academic |
DatabaseTitleList | MEDLINE - Academic MEDLINE CrossRef Engineering Research Database |
Database_xml | – sequence: 1 dbid: ECM name: MEDLINE url: https://search.ebscohost.com/login.aspx?direct=true&db=cmedm&site=ehost-live sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Engineering Chemistry Biology Anatomy & Physiology |
EISSN | 1097-0290 |
EndPage | 430 |
ExternalDocumentID | 10_1002_bit_1076 11320513 1102374 BIT1076 ark_67375_WNG_JZDJZ9P4_6 |
Genre | shortCommunication Research Support, Non-U.S. Gov't Journal Article |
GrantInformation_xml | – fundername: the Netherlands Ministry of Economic Affairs – fundername: the Russian Foundation for Basic Research funderid: 00‐04‐48658 – fundername: the Moscow City Government funderid: Gb‐18/9 |
GroupedDBID | --- -~X .3N .GA .GJ .Y3 05W 0R~ 10A 1L6 1OB 1OC 1ZS 23N 31~ 33P 3SF 3WU 4.4 4ZD 50Y 50Z 51W 51X 52M 52N 52O 52P 52S 52T 52U 52W 52X 53G 5GY 5RE 5VS 66C 702 7PT 8-0 8-1 8-3 8-4 8-5 8UM 930 A03 AAESR AAEVG AAHHS AANLZ AAONW AASGY AAXRX AAZKR ABCQN ABCUV ABIJN ABJNI ABPVW ACAHQ ACBWZ ACCFJ ACCZN ACGFO ACGFS ACIWK ACPOU ACPRK ACXBN ACXQS ADBBV ADEOM ADIZJ ADKYN ADMGS ADOZA ADXAS ADZMN ADZOD AEEZP AEIGN AEIMD AENEX AEQDE AEUQT AEUYR AFBPY AFFNX AFFPM AFGKR AFPWT AFRAH AFZJQ AHBTC AI. AIAGR AITYG AIURR AIWBW AJBDE AJXKR ALAGY ALMA_UNASSIGNED_HOLDINGS ALUQN AMBMR AMYDB ASPBG ATUGU AUFTA AVWKF AZBYB AZFZN AZVAB BAFTC BDRZF BFHJK BHBCM BMNLL BMXJE BNHUX BROTX BRXPI BSCLL BY8 CS3 D-E D-F DCZOG DPXWK DR1 DR2 DRFUL DRSTM DU5 EBS EJD F00 F01 F04 F5P FEDTE G-S G.N GNP GODZA H.T H.X HBH HGLYW HHY HHZ HVGLF HZ~ IX1 J0M JPC KQQ LATKE LAW LC2 LC3 LEEKS LH4 LITHE LOXES LP6 LP7 LUTES LW6 LYRES MEWTI MK4 MRFUL MRSTM MSFUL MSSTM MXFUL MXSTM N04 N05 N9A NF~ NNB O66 O9- OIG P2P P2W P2X P4D PQQKQ Q.N Q11 QB0 QRW R.K RBB RNS ROL RWI RX1 SUPJJ TN5 UB1 V2E VH1 W8V W99 WBKPD WH7 WIB WIH WIK WJL WNSPC WOHZO WQJ WRC WXSBR WYISQ XG1 XPP XSW XV2 Y6R ZZTAW ~02 ~IA ~KM ~WT 08R 3EH AAJUZ AAPBV ABCVL ABEML ABHUG ACSCC ACSMX ACXME ADAWD ADDAD AFVGU AGJLS BLYAC EBD EMOBN HF~ IQODW LH6 NDZJH PALCI RIWAO RJQFR RYL SAMSI SV3 WSB XFK ZGI ZXP CGR CUY CVF ECM EIF NPM AAMNL AAYXX CITATION 7QO 8FD FR3 P64 7X8 |
ID | FETCH-LOGICAL-c4156-9bedf5407053fd3500568054c8fe12b885a864bd5f3b973e60f3f044ab4703e23 |
IEDL.DBID | 33P |
ISSN | 0006-3592 |
IngestDate | Fri Aug 16 20:27:32 EDT 2024 Fri Aug 16 07:38:24 EDT 2024 Thu Nov 21 21:03:15 EST 2024 Sat Sep 28 07:36:38 EDT 2024 Sun Oct 22 16:05:01 EDT 2023 Sat Aug 24 01:12:35 EDT 2024 Wed Oct 30 10:05:34 EDT 2024 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 5 |
Language | English |
License | CC BY 4.0 Copyright 2001 John Wiley & Sons, Inc. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c4156-9bedf5407053fd3500568054c8fe12b885a864bd5f3b973e60f3f044ab4703e23 |
Notes | the Moscow City Government - No. Gb-18/9 ArticleID:BIT1076 istex:F069664F2EF213B760406E5EB6E2531A32C52788 ark:/67375/WNG-JZDJZ9P4-6 the Russian Foundation for Basic Research - No. 00-04-48658 the Netherlands Ministry of Economic Affairs ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
PMID | 11320513 |
PQID | 18150564 |
PQPubID | 23462 |
PageCount | 5 |
ParticipantIDs | proquest_miscellaneous_70809200 proquest_miscellaneous_18150564 crossref_primary_10_1002_bit_1076 pubmed_primary_11320513 pascalfrancis_primary_1102374 wiley_primary_10_1002_bit_1076_BIT1076 istex_primary_ark_67375_WNG_JZDJZ9P4_6 |
PublicationCentury | 2000 |
PublicationDate | 5 June 2001 |
PublicationDateYYYYMMDD | 2001-06-05 |
PublicationDate_xml | – month: 06 year: 2001 text: 5 June 2001 day: 05 |
PublicationDecade | 2000 |
PublicationPlace | New York |
PublicationPlace_xml | – name: New York – name: New York, NY – name: United States |
PublicationTitle | Biotechnology and bioengineering |
PublicationTitleAlternate | Biotechnol. Bioeng |
PublicationYear | 2001 |
Publisher | John Wiley & Sons, Inc Wiley |
Publisher_xml | – name: John Wiley & Sons, Inc – name: Wiley |
References | Youshko MI, Švedas VK. 2000. Kinetics of ampicillin synthesis, catalyzed by penicillin acylase from E. coli, in homogeneous and heterogeneous systems. Quantitative characterization of nucleophile reactivity and mathematical modeling of the process. Biochemistry (MOSCOW) 65:1367-1375. Margolin AL, Švedas VK, Nys PS, Koltsova EV, Savitskaya EM, Berezin IV. 1978. Study of penicillin amidase from E. coli. pH-Dependence of the equilibrium constant for enzymatic hydrolysis of ampicillin. Antibiotiki 23:114-118. Švedas VK, Margolin AL, Sherstiuk SF, Klyosov AA, Berezin IV. 1977. Inactivation of soluble and immobilized penicillin amidase from E. coli by phenylmethylsulphonylfluoride: kinetic analysis and titration of the active sites. Bioorg Khim 3:546-553. Švedas VK, Margolin AL, Borisov IL, Berezin IV. 1980b. Kinetics of the enzymatic synthesis of benzylpenicillin. Enzyme Microb Technol 2:313-317. Golobolov MYu, Borisov IL, Švedas VK. 1989. Acyl group transfer by proteases forming an acyl enzyme intermediate: kinetic model analysis (including hydrolysis of acyl enzyme-nucleophile complex). J Theor Biol 140:193-204. Schroën CGPH, Nierstrasz VA, Kroon PJ, Bosma R, Janssen AEM, Beeftink HH, Tramper J. 1999. Thermodynamically controlled synthesis of β-lactam antibiotics. Equilibrium concentrations and side-chain properties. Enzyme Microb Technol 24:498-506. Cole M. 1969. Factors affecting the synthesis of ampicillin and hydroxypenicillins by the cell-bound penicillin acylase of E. coli. Biochem J 115:757-764. Youshko MI, Van Langen LM, De Vroom E, Moody HM, Van Rantwijk F, Sheldon RA, Švedas VK. 2000. Penicillin acylase catalyzed synthesis of ampicillin in "aqueous solution-precipitate" systems. High reactants concentration and supersaturation effects. J Mol Catal B: Enzym 10:509-515. Hyun CK, Kim JH, Kim YJ. 1989. Effect of water activity on enzymatic synthesis of cephalexin. Biotechnol Lett 11:537-540. Bruggink A, Roos EC, De Vroom E. 1998. Penicillin acylase in the industrial production of β-lactam antibiotics. Org Process Res Dev 2:128-133. Fernandez-Lafuente R, Rosell CM, Guisan JM. 1998. The presence of methanol exerts a strong and complex modulation of the synthesis of different antibiotics by immobilized penicillin-G acylase. Enzyme Microb Technol 23:305-310. Margolin AL, Švedas VK, Berezin IV. 1980. Substrate specificity of penicillin amidase from E. coli. Biochim Biophys Acta 616:283-289. Boccu E, Ebert C, Gardossi L, Gianferrara T, Zacchigna M, Linda P. 1991. Enzymatic synthesis of ampicillin: a chemometric optimization. Farmaco 46:565-577. Kasche V, Haufler U, Zollner R. 1984. Kinetic studies on the mechanism of the penicillin amidase-catalysed synthesis of ampicillin and benzylpenicillin. Hoppe-Seyler Z Physiol Chem 365:1435-1443. Švedas VK, Margolin AL, Berezin IV. 1980a. Enzymatic synthesis of β-lactam antibiotics: a thermodynamic background. Enzyme Microb Technol 2:138-144. Diender MB, Straathof AJJ, Van der Wielen LAM, Ras C, Heijnen JJ. 1998. Feasibility of the thermodynamically controlled synthesis of amoxicillin. J Mol Catal B: Enzym 5:249-253. Kasche V, Galunsky B. 1982. Ionic strength and pH effects in the kinetically controlled synthesis of benzylpenicillin by nucleophilic deacylation of free and immobilized phenylacetyl-penicillin amidase with 6-aminopenicillanic acid. Biochem Biophys Res Commun 4:1215-1222. Ospina S, Barzana E, Ramirez OT, Lopez-Munquia A. 1996. Effect of pH in the synthesis of ampicillin by penicillin acylase. Enzyme Microb Technol 19:462-469. Van Langen LM, De Vroom E, Van Rantwijk F, Sheldon RA. 1999. Enzymatic synthesis of β-lactam antibiotics using penicillin-G acylase in frozen media. FEBS Lett 456:89-92. Kim MG, Lee SB. 1996. Penicillin acylase-catalyzed synthesis of pivampicillin: effect of reaction variables and organic cosolvents. J Mol Catal B: Enzym 1:71-80. 1989; 11 1980; 616 1996; 19 1978; 23 1991; 46 1984; 365 2000; 65 2000; 10 1980c 1982; 4 1998 1999; 24 1977; 3 1980a; 2 1996 1989; 140 1998; 2 1996; 1 1980b; 2 1969; 115 1998; 5 1999; 456 1998; 23 Margolin AL (e_1_2_1_14_1) 1978; 23 Švedas VK (e_1_2_1_22_1) 1980 Boccu E (e_1_2_1_2_1) 1991; 46 e_1_2_1_7_1 Švedas VK (e_1_2_1_19_1) 1977; 3 e_1_2_1_8_1 e_1_2_1_20_1 e_1_2_1_5_1 e_1_2_1_6_1 e_1_2_1_3_1 e_1_2_1_12_1 e_1_2_1_23_1 e_1_2_1_4_1 e_1_2_1_13_1 e_1_2_1_24_1 e_1_2_1_10_1 e_1_2_1_21_1 e_1_2_1_11_1 e_1_2_1_16_1 e_1_2_1_17_1 e_1_2_1_25_1 e_1_2_1_15_1 e_1_2_1_9_1 e_1_2_1_18_1 |
References_xml | – volume: 2 start-page: 128 year: 1998 end-page: 133 article-title: Penicillin acylase in the industrial production of β‐lactam antibiotics publication-title: Org Process Res Dev – volume: 23 start-page: 114 year: 1978 end-page: 118 article-title: Study of penicillin amidase from . pH‐Dependence of the equilibrium constant for enzymatic hydrolysis of ampicillin publication-title: Antibiotiki – volume: 616 start-page: 283 year: 1980 end-page: 289 article-title: Substrate specificity of penicillin amidase from publication-title: Biochim Biophys Acta – volume: 140 start-page: 193 year: 1989 end-page: 204 article-title: Acyl group transfer by proteases forming an acyl enzyme intermediate: kinetic model analysis (including hydrolysis of acyl enzyme‐nucleophile complex) publication-title: J Theor Biol – volume: 2 start-page: 313 year: 1980b end-page: 317 article-title: Kinetics of the enzymatic synthesis of benzylpenicillin publication-title: Enzyme Microb Technol – start-page: 257 year: 1980c end-page: 293 – volume: 2 start-page: 138 year: 1980a end-page: 144 article-title: Enzymatic synthesis of β‐lactam antibiotics: a thermodynamic background publication-title: Enzyme Microb Technol – volume: 4 start-page: 1215 year: 1982 end-page: 1222 article-title: Ionic strength and pH effects in the kinetically controlled synthesis of benzylpenicillin by nucleophilic deacylation of free and immobilized phenylacetyl‐penicillin amidase with 6‐aminopenicillanic acid publication-title: Biochem Biophys Res Commun – volume: 5 start-page: 249 year: 1998 end-page: 253 article-title: Feasibility of the thermodynamically controlled synthesis of amoxicillin publication-title: J Mol Catal B: Enzym – volume: 1 start-page: 71 year: 1996 end-page: 80 article-title: Penicillin acylase‐catalyzed synthesis of pivampicillin: effect of reaction variables and organic cosolvents publication-title: J Mol Catal B: Enzym – volume: 3 start-page: 546 year: 1977 end-page: 553 article-title: Inactivation of soluble and immobilized penicillin amidase from by phenylmethylsulphonylfluoride: kinetic analysis and titration of the active sites publication-title: Bioorg Khim – volume: 456 start-page: 89 year: 1999 end-page: 92 article-title: Enzymatic synthesis of β‐lactam antibiotics using penicillin‐G acylase in frozen media publication-title: FEBS Lett – year: 1996 – volume: 11 start-page: 537 year: 1989 end-page: 540 article-title: Effect of water activity on enzymatic synthesis of cephalexin publication-title: Biotechnol Lett – volume: 115 start-page: 757 year: 1969 end-page: 764 article-title: Factors affecting the synthesis of ampicillin and hydroxypenicillins by the cell‐bound penicillin acylase of publication-title: Biochem J – volume: 24 start-page: 498 year: 1999 end-page: 506 article-title: Thermodynamically controlled synthesis of β‐lactam antibiotics. Equilibrium concentrations and side‐chain properties publication-title: Enzyme Microb Technol – volume: 65 start-page: 1367 year: 2000 end-page: 1375 article-title: Kinetics of ampicillin synthesis, catalyzed by penicillin acylase from E. coli, in homogeneous and heterogeneous systems. Quantitative characterization of nucleophile reactivity and mathematical modeling of the process publication-title: Biochemistry (MOSCOW) – volume: 46 start-page: 565 year: 1991 end-page: 577 article-title: Enzymatic synthesis of ampicillin: a chemometric optimization publication-title: Farmaco – volume: 23 start-page: 305 year: 1998 end-page: 310 article-title: The presence of methanol exerts a strong and complex modulation of the synthesis of different antibiotics by immobilized penicillin‐G acylase publication-title: Enzyme Microb Technol – volume: 19 start-page: 462 year: 1996 end-page: 469 article-title: Effect of pH in the synthesis of ampicillin by penicillin acylase publication-title: Enzyme Microb Technol – volume: 10 start-page: 509 year: 2000 end-page: 515 article-title: Penicillin acylase catalyzed synthesis of ampicillin in “aqueous solution‐precipitate” systems. High reactants concentration and supersaturation effects publication-title: J Mol Catal B: Enzym – volume: 365 start-page: 1435 year: 1984 end-page: 1443 article-title: Kinetic studies on the mechanism of the penicillin amidase‐catalysed synthesis of ampicillin and benzylpenicillin publication-title: Hoppe‐Seyler Z Physiol Chem – year: 1998 – volume: 46 start-page: 565 year: 1991 ident: e_1_2_1_2_1 article-title: Enzymatic synthesis of ampicillin: a chemometric optimization publication-title: Farmaco contributor: fullname: Boccu E – ident: e_1_2_1_5_1 doi: 10.1016/S1381-1177(98)00044-7 – start-page: 257 volume-title: Enzyme engineering. Future directions year: 1980 ident: e_1_2_1_22_1 doi: 10.1007/978-1-4684-3719-5_8 contributor: fullname: Švedas VK – ident: e_1_2_1_9_1 doi: 10.1007/BF01040031 – ident: e_1_2_1_20_1 doi: 10.1016/0141-0229(80)90070-8 – ident: e_1_2_1_24_1 doi: 10.1023/A:1002896621567 – ident: e_1_2_1_6_1 doi: 10.1016/S0141-0229(98)00053-2 – ident: e_1_2_1_4_1 doi: 10.1042/bj1150757 – ident: e_1_2_1_25_1 doi: 10.1016/S1381-1177(00)00091-6 – volume: 3 start-page: 546 year: 1977 ident: e_1_2_1_19_1 article-title: Inactivation of soluble and immobilized penicillin amidase from E. coli by phenylmethylsulphonylfluoride: kinetic analysis and titration of the active sites publication-title: Bioorg Khim contributor: fullname: Švedas VK – ident: e_1_2_1_15_1 doi: 10.1016/0005-2744(80)90145-X – ident: e_1_2_1_16_1 – ident: e_1_2_1_23_1 doi: 10.1016/S0014-5793(99)00939-4 – ident: e_1_2_1_8_1 – ident: e_1_2_1_17_1 doi: 10.1016/S0141-0229(96)00032-4 – ident: e_1_2_1_7_1 doi: 10.1016/S0022-5193(89)80128-6 – ident: e_1_2_1_12_1 doi: 10.1515/bchm2.1984.365.2.1435 – ident: e_1_2_1_3_1 doi: 10.1021/op9700643 – ident: e_1_2_1_11_1 doi: 10.1016/0006-291X(82)91380-8 – ident: e_1_2_1_10_1 – ident: e_1_2_1_13_1 doi: 10.1016/1381-1177(95)00009-7 – ident: e_1_2_1_18_1 doi: 10.1016/S0141-0229(98)00140-9 – ident: e_1_2_1_21_1 doi: 10.1016/0141-0229(80)90103-9 – volume: 23 start-page: 114 year: 1978 ident: e_1_2_1_14_1 article-title: Study of penicillin amidase from E. coli. pH‐Dependence of the equilibrium constant for enzymatic hydrolysis of ampicillin publication-title: Antibiotiki contributor: fullname: Margolin AL |
SSID | ssj0007866 |
Score | 1.9453433 |
Snippet | The synthesis of ampicillin catalyzed by Escherichia coli penicillin acylase was optimized in an aqueous system with partially dissolved antibiotic nucleus... The synthesis of ampicillin catalyzed by Escherichia coli penicillin acylase was optimized in an aqueous system with partially dissolved antibiotic nucleus... |
SourceID | proquest crossref pubmed pascalfrancis wiley istex |
SourceType | Aggregation Database Index Database Publisher |
StartPage | 426 |
SubjectTerms | 6-aminopenicillanic acid ampicillin Ampicillin - metabolism ampicillin synthesis aqueous biocatalytic process aqueous solution-precipitate system Chemical Precipitation D-(-)-phenylglycine methyl ester Escherichia coli Escherichia coli - enzymology Models, Theoretical Penicillanic Acid - analogs & derivatives Penicillanic Acid - metabolism penicillin acylase Penicillin Amidase - metabolism Solutions Water |
Title | Highly efficient synthesis of ampicillin in an "aqueous solution-precipitate" system: Repetitive addition of substrates in a semicontinuous process |
URI | https://api.istex.fr/ark:/67375/WNG-JZDJZ9P4-6/fulltext.pdf https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fbit.1076 https://www.ncbi.nlm.nih.gov/pubmed/11320513 https://search.proquest.com/docview/18150564 https://search.proquest.com/docview/70809200 |
Volume | 73 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3daxQxEB-0IuqDH9fanlqNIH1buk02-9G3flr7UApWlL6EZDeBot07mh54b_cn-CroP3d_iTNJ99oDFUE4uOOYGy6ZyS8z2clvAN406EbOVjLReZ0nGRo20Zj9JDXXouSF5bmmc8iD98XRp3J3j2hyNru7MJEfYnbgRisj4DUtcG38-jVpqDkj9ueC2LYxSQi3N8TxDISLMj6mpIRZyIp3vLMpX-9-OLcT3aFJ_UqVkdrj5LjY1eJ3Yed8FBu2of1H_zOAx_DwKvhkW9FbnsAt2_ZgcavFxPt8zNZYKAcN5-w9uLvdfbq30zWF68GDG_yFi_CdqkS-jJkNPBS4fTE_bjGi9GeeDRzT50P8mki_Gb50y6aTHxqHORh51rn8dPJtSAQb1Lzk0k4nP1nklt5kmBrQDThEY0ZFTyRMSj0iXWDU9UEp81TdP6B-FyPSO4wXH5bgw_7eyc5BctXrIakphUwqYxtHZIAICq4RkihKSwwn69LZDW7KUuoyz0wjnTBVIWyeOuHSLNMmQ8yyXDyFhXbQ2hVgziJo1hLRCrNXjA-Nq3maGyMNrzYaK_vwurO7GkZKDxXJm7lCmyiySR_WgkPMBPTFZyqBK6T6ePRWHZ7uHp5Wx5lCwdU5j7nWSJwYRdaHV50HKTQVPY3RLc2zwtCKos-_SBQYzVeIYn1Yjq53Q7ngiKYC_2bwsD-OQ22_O6H3Z_8q-Bzuxyq7PEnlC1i4vBjZVbjtm9HLsMB-Ad26LIk |
link.rule.ids | 315,782,786,1408,27933,27934,46064,46488 |
linkProvider | Wiley-Blackwell |
linkToHtml | http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1ba1NBEB5si1QfvKReotauIH07NN09ey761KtpraFgROnLsnvOLhTtSehpwLzlJ_gq6J_LL3FmtydtQEUQAglhMmR3Zr-d2TP7DcDLEt3I2VxGOimSKEbDRhqzn6jgWmQ8tTzRdA7ZfZ_2PmW7e0ST87q5CxP4IWYHbrQyPF7TAqcD6Y0r1lBzSvTPabIAS3GCfkj3N8TxDIbTLDyopJRZyJw3zLMdvtH8cm4vWqJp_Uq1kbrG6XGhr8XvAs_5ONZvRPt3_2sI9-DOZfzJtoLD3IcbtmrBylaFuffZmK0zXxHqj9pbcHO7-bS80_SFa8HtaxSGK_CdCkW-jJn1VBS4g7F6XGFQWZ_WbOCYPhvi18T7zfClKzad_NA4zsGoZo3XTyffhsSxQf1LLux08pMFeulXDLMDugSHgMyo7omESWmNYOdJdWuvlNVU4D-glhcj0jsMdx8ewIf9vf5ON7ps9xAVlEVGubGlIz5AxAVXCkkspRlGlEXm7CY3WSZ1lsSmlE6YPBU26TjhOnGsTYywZbl4CIvVoLKPgTmLuFlIBCxMYDFENK7gncQYaXi-WVrZhheN4dUwsHqowN_MFdpEkU3asO49Yiagzz9TFVwq1cfeG3V4snt4kh_HCgVX51zmSiPRYqRxG9YaF1JoKnogoyuaZ4XRFQWgf5FIMaDPEcja8Cj43jXlgiOgCvyb3sX-OA61fdCn9yf_KrgGy93-uyN1dNB7-xRuhaK7JOrIZ7B4cT6yq7BQl6PnfrX9AqZ8MLE |
linkToPdf | http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1LaxsxEB6ahL4OfTh9uG0aFUpuSzbSah-5JXHcJC3G0JSWXIS0K0Fos16yMdQ3_4ReC-2f8y_pjDbrxNCWQsFgY8aDpRmNvtGOvgF4XaAbOZvJQMd5HERo2EBj9hPkXIuUJ5bHms4hD94ng09pb59ocrbbuzANP8T8wI1Who_XtMCrwm1ekYaaU2J_TuIlWIkQhRNvvhDDeRRO0uY5JWXMQma8JZ4N-Wb7y4WtaIVm9SuVRuoaZ8c1bS1-hzsXYazfh_r3_2cED-DeJfpkO427PIQbtuzA6k6JmffZhG0wXw_qD9o7cHO3_XR7r-0K14G71wgMV-E7lYl8mTDriShw_2L1pERIWZ_WbOSYPqvwa2L9ZvjSJZtNf2gc5mhcs9bnZ9NvFTFsUPeSCzub_mQNufQ2w9yArsBhOGZU9UTCpLTGUOcpdWuvlNVU3j-ihhdj0ls1Nx8ewYf-_vHeQXDZ7CHIKYcMMmMLR2yAGBVcISRxlKaIJ_PU2S1u0lTqNI5MIZ0wWSJsHDrhwijSJsKgZbl4DMvlqLRPgTmLUTOXGK4wfUWAaFzOw9gYaXi2VVjZhVet3VXVcHqohr2ZK7SJIpt0YcM7xFxAn3-mGrhEqo-DN-ropHd0kg0jhYJrCx5zpZFIMZKoC-utByk0FT2O0SXNs0JsRfDzLxIJwvkMw1gXnjSud0254BhOBf5N72F_HIfaPTym92f_KrgOt4a9vnp3OHj7HO40FXdxEMoXsHxxPrZrsFQX45d-rf0C3SIvVw |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Highly+efficient+synthesis+of+ampicillin+in+an+%E2%80%9Caqueous+solution%E2%80%90precipitate%E2%80%9D+system%3A+Repetitive+addition+of+substrates+in+a+semicontinuous+process&rft.jtitle=Biotechnology+and+bioengineering&rft.au=Youshko%2C+Maxim+I.&rft.au=van+Langen%2C+Luuk+M.&rft.au=de+Vroom%2C+Erik&rft.au=van+Rantwijk%2C+Fred&rft.date=2001-06-05&rft.pub=John+Wiley+%26+Sons%2C+Inc&rft.issn=0006-3592&rft.eissn=1097-0290&rft.volume=73&rft.issue=5&rft.spage=426&rft.epage=430&rft_id=info:doi/10.1002%2Fbit.1076&rft.externalDBID=10.1002%252Fbit.1076&rft.externalDocID=BIT1076 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0006-3592&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0006-3592&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0006-3592&client=summon |