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Cited by 23Enzyme Catalysis and ImmobilizationEnzyme Production and Characterizationthermodynamics and calorimetric analyses

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Kinetic model discrimination of penicillin G acylase thermal deactivation by non-isothermal continuous activity assay

McDonald, Matthew A., Bromig, Lukas, Grover, Martha A., Rousseau, Ronald W., Bommarius, Andreas S.·2018·Chemical Engineering Science
DOI 10.1016/j.ces.2018.04.046
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Crossref · 10.1016/j.ces.2018.04.046

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  • PGA has less than 1% deactivation over 100 min under the same conditions (25°C, pH 7.0) based on current deactivation data.

    “For comparison, PGA, a more readily used enzyme for synthesis of ß-lactam antibiotics, has <1% deactivation over 100 min under these conditions based on current deactivation data (McDonald et al., 2018).”

    From Reactor Design and Optimization of α-Amino Ester Hydrolase-Catalyzed Synthesis of Cephalexin (2022) · cites this paper as McDonald et al., 2018

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Research works printed but not linked: 27

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  2. Alkema, 2003, Kinetics of enzyme acylation and deacylation in the penicillin acylase-catalyzed synthesis of beta-lactam antibiotics, Eur. J. Biochem., 270, 3675, 10.1046/j.1432-1033.2003.03728.x · DOI
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  7. de los Ríos, 2007, Stabilization of native penicillin G acylase by ionic liquids, J. Chem. Technol. Biotechnol., 82, 190, 10.1002/jctb.1654 · DOI
  8. Deaguero, A.L., Blum, J.K., Bommarius, A.S., 2010, Biocatalytic synthesis of beta-lactam antibiotics. In: Flickinger, M. (Ed.). The Encyclopedia of Industrial Biotechnology: Bioprocess, Bioseparation, and Cell Technology, 2nd ed., pp 535–567, Wiley. · DOI
  9. Elander, 2003, Industrial production of β-lactam antibiotics, Appl. Microbiol. Biotechnol., 61, 385, 10.1007/s00253-003-1274-y · DOI
  10. Flores, 2004, Production of a fully functional, permuted single-chain penicillin G acylase, Protein Sci., 13, 1677, 10.1110/ps.03436604 · DOI
  11. Grinberg, 2008, Thermodynamic and kinetic stability of penicillin acylase from Escherichia coli, Biochim. et Biophys. Acta (BBA)-Proteins Proteomics, 1784, 736, 10.1016/j.bbapap.2008.01.016 · DOI
  12. Illanes, 1996, Thermal inactivation of immobilized penicillin acylase in the presence of substrate and products, Biotechnol. Bioeng., 50, 609, 10.1002/(SICI)1097-0290(19960620)50:6<609::AID-BIT1>3.0.CO;2-O · DOI
  13. Kazan, 1997, Stabilization ofEscherichia coli penicillin G acylase by polyethylene glycols against thermal inactivation, Appl. Biochem. Biotechnol., 62, 1, 10.1007/BF02787979 · DOI
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  16. Mazurenko, 2017, Exploration of protein unfolding by modelling calorimetry data from reheating, Sci. Rep., 7, 16321, 10.1038/s41598-017-16360-y · DOI
  17. McDonald, 2017, Enzymatic reactive crystallization for improving ampicillin synthesis, Chem. Eng. Sci., 165, 81, 10.1016/j.ces.2017.02.040 · DOI
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  27. Youshko, 2002, Quantitative characterization of the nucleophile reactivity in penicillin acylase-catalyzed acyl transfer reactions, Biochim. et Biophys. Acta (BBA)-Proteins Proteomics, 1599, 134, 10.1016/S1570-9639(02)00413-2 · DOI

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Metadata

Authors
McDonald, M. A., Bromig, L., Grover, M. A., Rousseau, R. W., & Bommarius, A. S.
Affiliations
Georgia Institute of Technology (US)
Corresponding author
Bommarius, Andreas S.
ORCID
Venue
Chemical Engineering Science
Publisher
Elsevier BV
Published
2018-09
Volume
187
Pages
79-86
ISSN
0009-2509 (ISSN-L)
DOI
10.1016/j.ces.2018.04.046
OpenAlex
W2802195015
Cited by
23
References
0
Citations by year
2026: 1 · 2024: 4 · 2023: 4 · 2022: 4 · 2021: 6 · 2020: 2 · 2019: 2
FWCI
0.89
Type
journal article
Language
en
Open access
closed
Licence
Locations
Chemical Engineering Science (publishedVersion)
Funders
Georgia Research Alliance
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Physical Sciences › Chemistry › Physical and Theoretical Chemistry › thermodynamics and calorimetric analyses
Keywords
penicillin G acylase, kinetic model discrimination, temperature profiles, Akaike information criterion, lysozyme, TEM-1 beta-lactamase, enzyme kinetics

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