Radiation-induced polymerization for the immobilization of penicillin acylase

Journal Article · Mon Jun 01 04:00:00 EDT 1987 · Appl. Biochem. Biotechnol.; (United States)

DOI:https://doi.org/10.1007/BF02798502· OSTI ID:5847815

Boccu, E; Carenza, M; Lora, S; Palma, G; Veronese, F M

The immobilization of Escherichia coli penicillin acylase was investigated by radiation-induced polymerization of 2-hydroxyethyl methacrylate at low temperature. A leak-proof composite that does not swell in water was obtained by adding the cross-linking agent trimethylolpropane trimethacrylate to the monomer-aqueous enzyme mixture. Penicillin acylase, which was immobilized with greater than 70% yield, possessed a higher Km value toward the substrate 6-nitro-3-phenylacetamidobenzoic acid than the free enzyme form (Km = 1.7 X 10(-5) and 1 X 10(-5) M, respectively). The structural stability of immobilized penicillin acylase, as assessed by heat, guanidinium chloride, and pH denaturation profiles, was very similar to that of the free-enzyme form, thus suggesting that penicillin acylase was entrapped in its native state into aqueous free spaces of the polymer matrix.

• Research Organization: Universita di Padova, Italy
• OSTI ID: 5847815
• Journal Information: Appl. Biochem. Biotechnol.; (United States), Journal Name: Appl. Biochem. Biotechnol.; (United States) Vol. 15:1; ISSN ABIBD
• Country of Publication: United States
• Language: English

Related Subjects

560130* -- Radiation Effects on Microorganisms
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
AMIDASES
BACTERIA
BIOLOGICAL EFFECTS
BIOLOGICAL RADIATION EFFECTS
CARBOXYLIC ACID SALTS
CHEMICAL REACTIONS
ENZYMES
ESCHERICHIA COLI
HYDROLASES
IMMOBILIZED ENZYMES
METHACRYLATES
MICROORGANISMS
NON-PEPTIDE C-N HYDROLASES
POLYMERIZATION
RADIATION EFFECTS
RADIOINDUCTION