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| rdf:type
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| Description
| - Penicillin G acylase from Achromobacter sp. (NPGA) was studied in the enzymatic synthesis of beta-lactam antibiotics by kinetically controlled N-acylation. When compared with penicillin acylase of Escherichia coli (PGA), the NPGA was significantly more efficient at syntheses of ampicillin and amoxicillin (higher S/H ratio and product accumulation) in the whole range of substrate concentrations. The degree of conversion of 6-aminopenicillanic acid to amoxicillin and ampicillin (160 mM 6-APA, 350 mM acyl donor methylestera <...HCl, pH 6.3, 25 A degrees C, reaction time of 200 min) with immobilized NPGA equaled 96.9 % and 91.1 %, respectively. The enzyme was highly thermostable with maximum activity at 60 A degrees C (pH 8.0) and 65 A degrees C (pH 6.0). Activity half-life at 60 A degrees C (pH 8.0) and at 60 A degrees C (pH 6.0) was 24 min and 6.9 h, respectively. Immobilized NPGA exhibited long operational stability with half-life of about 2,000 cycles for synthesis of amoxicillin at conversion conditions used in large-scale processes (230 mM 6-APA, 340 mM d-4-hydroxyphenylglycine methylestera <...HCl, 27.5 A degrees C, pH 6.25). We discuss our results with literature data available for related penicillin acylases in terms of their industrial potential
- Penicillin G acylase from Achromobacter sp. (NPGA) was studied in the enzymatic synthesis of beta-lactam antibiotics by kinetically controlled N-acylation. When compared with penicillin acylase of Escherichia coli (PGA), the NPGA was significantly more efficient at syntheses of ampicillin and amoxicillin (higher S/H ratio and product accumulation) in the whole range of substrate concentrations. The degree of conversion of 6-aminopenicillanic acid to amoxicillin and ampicillin (160 mM 6-APA, 350 mM acyl donor methylestera <...HCl, pH 6.3, 25 A degrees C, reaction time of 200 min) with immobilized NPGA equaled 96.9 % and 91.1 %, respectively. The enzyme was highly thermostable with maximum activity at 60 A degrees C (pH 8.0) and 65 A degrees C (pH 6.0). Activity half-life at 60 A degrees C (pH 8.0) and at 60 A degrees C (pH 6.0) was 24 min and 6.9 h, respectively. Immobilized NPGA exhibited long operational stability with half-life of about 2,000 cycles for synthesis of amoxicillin at conversion conditions used in large-scale processes (230 mM 6-APA, 340 mM d-4-hydroxyphenylglycine methylestera <...HCl, 27.5 A degrees C, pH 6.25). We discuss our results with literature data available for related penicillin acylases in terms of their industrial potential (en)
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| Title
| - Penicillin G acylase from Achromobacter sp CCM 4824 An efficient biocatalyst for syntheses of beta-lactam antibiotics under conditions employed in large-scale processes
- Penicillin G acylase from Achromobacter sp CCM 4824 An efficient biocatalyst for syntheses of beta-lactam antibiotics under conditions employed in large-scale processes (en)
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| skos:prefLabel
| - Penicillin G acylase from Achromobacter sp CCM 4824 An efficient biocatalyst for syntheses of beta-lactam antibiotics under conditions employed in large-scale processes
- Penicillin G acylase from Achromobacter sp CCM 4824 An efficient biocatalyst for syntheses of beta-lactam antibiotics under conditions employed in large-scale processes (en)
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| skos:notation
| - RIV/61388971:_____/14:00428440!RIV15-AV0-61388971
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| http://linked.open...avai/riv/aktivita
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| http://linked.open...avai/riv/aktivity
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
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| http://linked.open...aciTvurceVysledku
| - Maršálek, Jaroslav
- Bečka, Stanislav
- Plháčková, Kamila
- Kyslík, Pavel
- Štěpánek, Václav
- Dobišová, Marie
- Grulich, Michal
- Valešová, Renata
- Marešová, Helena
- Palyzová, Andrea
- Plačková, Martina
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
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| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
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| http://linked.open...ai/riv/idVysledku
| - RIV/61388971:_____/14:00428440
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| http://linked.open...riv/jazykVysledku
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| http://linked.open.../riv/klicovaSlova
| - Achromobacter sp.; Penicillin G acylase; beta-Lactam antibiotics (en)
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| http://linked.open.../riv/klicoveSlovo
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| http://linked.open...odStatuVydavatele
| - DE - Spolková republika Německo
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| http://linked.open...ontrolniKodProRIV
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| http://linked.open...i/riv/nazevZdroje
| - Applied Microbiology and Biotechnology
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| http://linked.open...in/vavai/riv/obor
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| http://linked.open...ichTvurcuVysledku
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| http://linked.open...cetTvurcuVysledku
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| http://linked.open...UplatneniVysledku
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| http://linked.open...v/svazekPeriodika
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| http://linked.open...iv/tvurceVysledku
| - Bečka, Stanislav
- Datla, A.
- Kyslík, Pavel
- Maršálek, Jaroslav
- Plháčková, Kamila
- Vyasarayani, W. R.
- Štěpánek, Václav
- Grulich, Michal
- Marešová, Helena
- Palyzová, Andrea
- Valešová, Renata
- Plačková, Martina
- Dobišová, Marie
- Ashar, T. K.
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| http://linked.open...ain/vavai/riv/wos
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| issn
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| number of pages
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| http://bibframe.org/vocab/doi
| - 10.1007/s00253-013-4945-3
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