Purified penicillin acylase performance in a stabilized ultrafiltration membrane reactor

Greco, Guido; Veronese, Francesco M.; Largajolli, Roberta; Gianfreda, Liliana

doi:10.1007/bf00504741

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Biocatalyst Production1

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Cited by 20 publications

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“…The stability of the catalyst produced is adequate for practical applications. ( Greco et al, 1983), 2 (Ospina et al, 1992), 3(this work) Finally, the whole cell biocatalyst was applied to the hydrolysis of penicillin to obtain 6-APA ( Figure 100. Figure 3.…”

Section: Biocatalyst Productionmentioning

confidence: 99%

Recombinant whole cell penicillin acylase biocatalyst: Production, characterization and use in the synthesis and hydrolysis of antibiotics

et al. 1995

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Section: Biocatalyst Productionmentioning

confidence: 99%

Recombinant whole cell penicillin acylase biocatalyst: Production, characterization and use in the synthesis and hydrolysis of antibiotics

et al. 1995

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Thermal inactivation of immobilized penicillin acylase in the presence of substrate and products

Illanes

Altamirano

Zúñiga

1996

Biotechnol. Bioeng.

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Penicillin acylase release from Escherichia coli cells by mechanical cell disruption and permeabilization

Fonseca

2002

J of Chemical Tech & Biotech

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The release of Penicillin acylase from Escherichia coli cells through mechanical cell disruption using high-pressure homogenization and sonication was studied. From these cell disruption processes, the enzyme activity was totally released although with low speci®c activities, 0.1±0.3 IU(mg prot) À1. Intracellular total soluble protein release was quanti®ed and modelled by a ®rst order kinetic model. The effect of the driving force for each mechanical method, namely acoustic power input and homogenization pressure, on the respective kinetic disruption constants was also analysed. The release of Penicillin acylase by cell permeabilization using osmotic shock was also evaluated. The effects of cell concentration, penicillin acylase activity in E coli cells, type of buffer, pH, hypertonic solution composition, temperature and time used for osmotic shock were evaluated. Using cold osmotic shock, highly selective penicillin acylase release was attained with speci®c enzyme activities of about 4 IU(mg prot)À1 and enzyme activity release yields higher than 90%. The high purity of the penicillin acylase was a consequence of the optimized differential enzyme release method which was validated by SDS gel electrophoresis.

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Purified penicillin acylase performance in a stabilized ultrafiltration membrane reactor

Cited by 20 publications

References 11 publications

Recombinant whole cell penicillin acylase biocatalyst: Production, characterization and use in the synthesis and hydrolysis of antibiotics

Recombinant whole cell penicillin acylase biocatalyst: Production, characterization and use in the synthesis and hydrolysis of antibiotics

Thermal inactivation of immobilized penicillin acylase in the presence of substrate and products

Penicillin acylase release from Escherichia coli cells by mechanical cell disruption and permeabilization

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