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Stabilisation and immobilisation of penicillin amidase.

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Burteau, Nathalie [UCL] Burton, S Crichton, Robert [UCL]

Penicillin amidase was coupled to a periodate-oxidised dextran by reductive alkylation in the presence of sodium cyanoborohydride. A loss of activity (25%) was observed but the conjugate enzyme dextran was more thermostable than the native enzyme. Native and dextran-conjugated penicillin amidase were immobilised on amino activated silica (Promaxon, Spherosil, Aerosil) by a classical method using glutaraldehyde for the native enzyme and reductive alkylation for the modified enzyme. Good relative activity of the enzymes was obtained after insolubilisation. Immobilisation of both native and modified enzymes resulted in the thermostabilisation of the penicillin amidase.

Document type Article de périodique (Journal article) – Comparative Study, Journal Article
Publication date 1989
Journal information "FEBS letters" - Vol. 258, no. 2, p. 185-9 (1989)
Peer reviewed yes
issn 0014-5793
Publication status Publié
Affiliation UCL - SC/CHIM - Département de chimie
MESH Subject Enzyme Stability ; Enzymes, Immobilized - metabolism ; Escherichia coli - enzymology ; Kinetics ; Penicillinase - isolation & purification - metabolism ; Thermodynamics
Links
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Bibliographic reference Burteau, Nathalie ; Burton, S ; Crichton, Robert. Stabilisation and immobilisation of penicillin amidase.. In: FEBS letters, Vol. 258, no. 2, p. 185-9 (1989)
Permanent URL http://hdl.handle.net/2078.1/11637