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Stability and stabilisation of penicillin acylase

✍ Scribed by Ana M Azevedo; Luís P Fonseca; Duarte M F Prazeres

Publisher
Wiley (John Wiley & Sons)
Year
1999
Tongue
English
Weight
137 KB
Volume
74
Category
Article
ISSN
0268-2575

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✦ Synopsis

The stability of an oligomeric enzyme, penicillin acylase, was studied in aqueous media. The enzyme was produced by mutant cells of Escherichia coli ATCC 9637, extracted from the periplasmic space by osmotic shock and further puri®ed using a pseudo-af®nity adsorption process. Enzyme stabilisation attempts were performed with salts, alcohols and sugars. The highest levels of retained activity were obtained in the presence of 15% (w/v) ammonium or sodium sulfate. A kinetic model was proposed to describe the inactivation of penicillin acylase, taking into account results obtained in stability assays performed at different temperatures and with different enzyme concentrations. According to this model, the inactivation of penicillin acylase involves an intermediary active precursor of the enzyme, formed prior to dissociation into sub-units.

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