Results 141 to 150 of about 6,518 (178)

The penicillin amidase of Arthrobacter viscosus (ATCC 15294)

Gene, 1994
The nucleotide (nt) sequence of the gene encoding penicillin G amidase (PA) of Arthrobacter viscosus strain ATCC 15,294 was determined. The sequence contained an open reading frame of 2406 nt with a G+C content of 37%. The deduced amino-acid sequence shows significant homology with other so far identified beta-lactam amidases of Gram- bacteria.
M, Konstantinović, N, Marjanović, G, Ljubijankić, V, Glisin   +3 more
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Hydrophobic interaction chromatography of penicillin amidase

Biotechnology Letters, 1987
For hydrophobic binding of penicillin amidase to modified Sepharose, a phenyl group or a hydrophobic aliphatic moiety (leucyl, octyl) is necessary. Concentration and purification of the enzyme can then be achieved in a single step.
Vayalombron K. Sudhakaran, Jaiprakash G. Shewale   +1 more
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A Colorimetric Assay for Penicillin-V Amidase

Analytical Biochemistry, 1993
The hydrolysis of penicillin-V to phenoxyacetic acid and 6-aminopenicillanic acid by the fungal enzyme penicillin-V amidase is of industrial importance since the 6-aminopenicillanic acid produced is an intermediate for semisynthetic penicillins. A rapid colorimetric assay of penicillin-V amidase was developed which uses 2-nitro-5-(phenoxyacetamido ...
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The isolation and kinetics of penicillin amidase from Escherichia coli

Biochimica et Biophysica Acta (BBA) - Enzymology, 1972
Abstract 1. 1. A penicillin amidase (penicillin amidohydrolase, EC 3.5.1.11) was extracted from Escherichia coli NCIB 8743A and purified by precipitation first with (NH 4 ) 2 SO 4 and then polyethyleneglycol, followed by chromatography on DEAE-cellulose. 2. 2.
K, Balasingham, D, Warburton, P, Dunnill, M D, Lilly   +3 more
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Penicillin amidase production by bacillus megaterium

Biotechnology and Bioengineering, 1973
AbstractPenicillin amidase, an enzyme which hydrolyzes benzylpenicillin to 6‐aminopenicillanic acid and phenylacetic acid, is produced by Bacillus megaterium ATCC 14945 as an extracellular enzyme. We used this system as a model to examine the effects of nitrogen, sulfur, and phosphorous limitation on enzyme production in continuous culture.
F, Acevedo, C L, Cooney
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Penicillin G sensor based on penicillin amidase coupled to a field effect transistor

Analytica Chimica Acta, 1989
Abstract A penicillin sensor for the rapid determination of penicillin G was developed. The basic element of this biosensor is a hydrogen ion-sensitive field effect transistor (pH-FET). The pH-sensitive surface of this device is modified with an immobilized penicillin amidase membrane layer.
U. Brand, T. Scheper, K. Schügerl
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The preparation and kinetics of immobilised penicillin amidase from Escherichia coli

Biochimica et Biophysica Acta (BBA) - Enzymology, 1972
1. 1.|Penicillin amidase (penicillin amidohydrolase, EC 3.5.1.11) has been immobilised by covalent binding to DEAE-cellulose using 2-amino-4,6-dichloro-s-triazine. 2. 2.|The immobilised penicillin amidase preparations contained up to 160 mg protein/g. DEAE-cellulose and the bound enzyme retained 45–81% of its activity before attachment.
D, Warburton, K, Balasingham, P, Dunnill, M D, Lilly   +3 more
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[Penicillin amidase from E. coli. A comparative study of the stability of penicillin amidase immobilized by various means].

Antibiotiki, 1977
The properties of immobilized penicillinamidases prepared by different methods were studied. Immobilization of penicillinamidase was achieved by using the covalend binding ion exchange sorption, incorporation into gel and other procedures. The effect of the carrier type, purification level of the native enzyme and other factors on stability of the ...
P S, Nys, E M, Savitskaia, N N, Shellenberg   +2 more
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Affinity and hydrophobic interactions of penicillin amidase.

Hindustan antibiotics bulletin, 1990
Binding of penicillin amidase from E. coli 436 to aniline-, benzylamine- and phenylethylamine-Sepharose was studied. Binding of the enzyme to aniline-Sepharose was exclusively due to hydrophobic interactions. Benzylamine-Sepharose binds the enzyme due to affinity interactions in the absence of ammonium sulphate and due to hydrophobic interactions in ...
R S, Mali, V K, Sudhakaran, J G, Shewale
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Effect of recycling of fermentation broth for the production of penicillin amidase

Process Biochemistry, 1991
Abstract In general in any fermentation the volume of wastewater is too high. The excess water might be utilized to reduce consumption of process water. In this investigation cell-free culture filtrate was used instead of process water. In batch experiments, cell-free culture filtrate was used in ratios between 0·1 and 1·0 for eight subsequent ...
P.S.R. Babu, T. Panda
openaire   +1 more source