Zobrazeno 1 - 10
of 51
pro vyhledávání: '"M I, Youshko"'
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 56:202-207
The microstructure and the catalytic properties of cross-linked enzyme aggregates (CLEA) of penicillin acylase (PA) obtained under different conditions were investigated. The period of time left between the enzyme precipitation and the cross-linking
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::abc80bf94c2691fe9a4a938cd3e2b96e
https://doi.org/10.1016/j.molcatb.2008.05.006
https://doi.org/10.1016/j.molcatb.2008.05.006
Publikováno v:
Tetrahedron: Asymmetry. 15:1933-1936
Aminoacylase I from Aspergillus melleus , a readily available and inexpensive enzyme mainly used in the industrial production of enantiopure l -amino acids from their N -acetyl derivatives, is shown to hydrolyze the esters and amides of natural and n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1c3c482e127974a4727a7c9651ce18d6
https://doi.org/10.1016/j.tetasy.2004.05.018
https://doi.org/10.1016/j.tetasy.2004.05.018
Autor:
Vytas K. Švedas, Wilhelmus H J Boosten, Alexander L Bukhanov, M. I. Youshko, Harold Monro Moody
Publikováno v:
Biotechnology and Bioengineering. 85:323-329
Advantages of performing penicillin acylase-catalyzed synthesis of new penicillins and cephalosporins by enzymatic acyl transfer to the beta-lactam antibiotic nuclei in the supersaturated solutions of substrates have been demonstrated. It has been sh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::168923ec152165a19525363d84852c67
https://doi.org/10.1002/bit.10863
https://doi.org/10.1002/bit.10863
Publikováno v:
Biochemistry (Moscow). 68:334-338
The influence of the external nucleophile (6-aminopenicillanic acid) on the kinetics of the penicillin acylase-catalyzed acyl transfer reactions was studied using a highly sensitive spectrophotometric assay. An adequate kinetic scheme is suggested ba
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::38d0c35b201fc707d4333596e984e2dc
https://doi.org/10.1023/a:1023014519139
https://doi.org/10.1023/a:1023014519139
Autor:
M. I. Youshko, Vytas K. Švedas
Publikováno v:
Advanced Synthesis & Catalysis. 344:894-898
The ability of immobilized penicillin acylase from E. coli to retain a remarkable catalytic activity in solid-state systems has been demonstrated. Stabilization of immobilized penicillin acylase by inorganic salt hydrates allowed us to exploit nearly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7a634d60d9022813209b09cc44aec208
https://doi.org/10.1002/1615-4169(200209)344:8<894::aid-adsc894>3.0.co
https://doi.org/10.1002/1615-4169(200209)344:8<894::aid-adsc894>3.0.co
Autor:
Erik de Vroom, Fred van Rantwijk, Roger A. Sheldon, Luuk M. van Langen, M. I. Youshko, Vytas K. Švedas
Publikováno v:
Biotechnology and Bioengineering. 78:589-593
The penicillin acylase-catalyzed synthesis of ampicillin by acyl transfer from D-(-)-phenylglycine amide (D-PGA) to 6-aminopenicillanic acid (6-APA) becomes more effective when a judiciously chosen pH gradient is applied in the course of the process.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::173d1f64a4a2b3627b4cdfe057dba6cc
https://doi.org/10.1002/bit.10234
https://doi.org/10.1002/bit.10234
Autor:
M. I. Youshko, Luuk M. van Langen, Vytas K. Švedas, Fred van Rantwijk, Harold Monro Moody, Erik de Vroom, Roger A. Sheldon
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 10:509-515
Penicillin acylase-catalyzed ampicillin synthesis via acyl group transfer in aqueous solution is highly dependent on the initial substrate concentration. The solubility of one substrate, 6-aminopenicillanic acid (6-APA), can be advantageously enhance
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c5145e0ea4481a88f0f06e4bffc0e94e
https://doi.org/10.1016/s1381-1177(00)00091-6
https://doi.org/10.1016/s1381-1177(00)00091-6
Autor:
Vytas K. Švedas, M. I. Youshko
Publikováno v:
Biochemistry (Moscow). 65:1367-1375
Kinetic regularities of the enzymatic acyl group transfer reactions have been studied using ampicillin synthesis catalyzed by E. coli penicillin acylase as an example. It was shown that ampicillin synthesis proceeds through the formation of an acylen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1aa068167732a4d4af44942d67b02e9a
https://doi.org/10.1023/a:1002896621567
https://doi.org/10.1023/a:1002896621567
Publikováno v:
Biochemistry. Biokhimiia. 71(3)
A new method for monitoring reactions catalyzed by an immobilized enzyme, cross-linked penicillin acylase aggregates (PA CLEA), is suggested. Appropriate chromogenic substrates for spectrophotometric assay of catalytic activity of immobilized enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b0b1b8a2ec9ee123ee51d98791d521b
https://pubmed.ncbi.nlm.nih.gov/16545069
https://pubmed.ncbi.nlm.nih.gov/16545069
Publikováno v:
Biochemistry. Biokhimiia. 68(3)
The influence of the external nucleophile (6-aminopenicillanic acid) on the kinetics of the penicillin acylase-catalyzed acyl transfer reactions was studied using a highly sensitive spectrophotometric assay. An adequate kinetic scheme is suggested ba
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fd83d81897b82fc75c4247bfa8e33243
https://pubmed.ncbi.nlm.nih.gov/12733976
https://pubmed.ncbi.nlm.nih.gov/12733976