Results 151 to 160 of about 6,518 (178)
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Biotechnology and Bioengineering, 1969
AbstractPenicillin amidase was extracted from Escherichia coli ATCC 9637, grown on phenylacetic, acid and glutamate, and purified by fractional ion with streptomycin sulphate, ammonium sulphate and polyethylene glycol, followed by chromatography on DEAE–cellulose. The purification factor was 100–200 × and the overall yield was about 115%.
A, Self, G, Kay, M D, Lilly, P, Dunnill
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AbstractPenicillin amidase was extracted from Escherichia coli ATCC 9637, grown on phenylacetic, acid and glutamate, and purified by fractional ion with streptomycin sulphate, ammonium sulphate and polyethylene glycol, followed by chromatography on DEAE–cellulose. The purification factor was 100–200 × and the overall yield was about 115%.
A, Self, G, Kay, M D, Lilly, P, Dunnill
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1978
In the last few years improvements in enzyme immobilization techniques have enabled enzymatic hydrolysis of penicillin G for the production of 6APA to become a viable alternative to chemical hydrolysis. This paper presents a novel process method for producing 6APA by enzymatic hydrolysis.
F. Giacobbe, A. Iasonna, F. Cecer
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In the last few years improvements in enzyme immobilization techniques have enabled enzymatic hydrolysis of penicillin G for the production of 6APA to become a viable alternative to chemical hydrolysis. This paper presents a novel process method for producing 6APA by enzymatic hydrolysis.
F. Giacobbe, A. Iasonna, F. Cecer
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[Properties of penicillin amidase covalently bound to cellulose matrices].
Antibiotiki, 1976Properties of penicillinamidase (PA) covalently bound with the cellulose matrix were studied. The efficiency of the binding depended on the bind type and purity of the native enzyme taken for binding. Stability of the immobilized PA (IPA) was studied at wide pH ranges.
P S, Nys +3 more
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Enzyme-linked immunosorbent assay (ELISA) of penicillin amidases.
Archivum immunologiae et therapiae experimentalis, 1987Non-competitive, sandwich enzyme immunoassay for both penicillin amidases from Escherichia coli is described. The assay involves the use of monospecific antibodies and their conjugates. The amidases inactivated by heating and by acid- or alkali-treatment cannot be assayed.
E, Prusak, J, Wieczorek, A, Szewczuk
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Penicillin Amidase from E. coli
Annals of the New York Academy of Sciences, 1987V, Kasche +5 more
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A substrate susceptivity screening on penicillin amidase
Biotechnology Letters, 1994openaire +1 more source
3D-QSAR Applied to the Quantitative Prediction of Penicillin G Amidase Selectivity
Advanced Synthesis and Catalysis, 2006Paolo Braiuca +2 more
exaly