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Applied Microbiology and Biotechnology, 2016
Enzymatic penicillin hydrolysis by penicillin amidase (also penicillin acylase, PA) represents a Landmark: the first industrially and economically highly important process using an immobilized biocatalyst. Resistance of infective bacteria to antibiotics had become a major topic of research and industrial activities.
Klaus Buchholz
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Enzymatic penicillin hydrolysis by penicillin amidase (also penicillin acylase, PA) represents a Landmark: the first industrially and economically highly important process using an immobilized biocatalyst. Resistance of infective bacteria to antibiotics had become a major topic of research and industrial activities.
Klaus Buchholz
exaly +3 more sources
Substrate specificity of penicillin amidase from E. coli
Biochimica Et Biophysica Acta - Biomembranes, 19801. The kinetic parameters of 12 substrates of penicillin amidase (penicillin amidohydrolase, EC 3.5.1.11) from E. coli have been determined. Most of the penicillin amidase amide substrates containing a phenylacetyl group in the acyl moiety have been shown to have similar catalytic constants of 50 s-1.
Alexey L Margolin +2 more
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Preparation and properties of penicillin amidase immobilized in polyelectrolyte complexes
Biochimica Et Biophysica Acta - Biomembranes, 1981Abstract (1) Immobilization of penicillin amidase (acylamide amidohydrolase, EC 3.5.1.4) from Escherichia coli was carried out on negatively charged particles of the water-soluble polyelectrolyte complex formed by poly(4-vinyl- N -ethylpyridinium bromide) and poly(methacrylic acid) in the ratio 1 : 3.
A L Margolin +2 more
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pH dependence of penicillin amidase enantioselectivity for charged substrates
BBA - Proteins and Proteomics, 1999The pH dependence of E (enantiomeric ratio or enantioselectivity, a quantitative measure for enzyme stereospecificity) was studied for penicillin amidase catalysed hydrolysis of charged enantiomeric substrates. Theoretical analysis shows that a pH dependence can only be observed around the pK values of groups in the active site whose ionisation control
Boris Galunsky, V Kasche, B Galunsky
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Activity of immobilised penicillin amidase in toluene at controlled water activity
Journal of Molecular Catalysis B: Enzymatic, 1998J. MOL. CATAL.
Cynthia Ebert +2 more
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Production of glycosylated thermostable penicillin G amidase in
FEMS Yeast Research, 2002Vittorio Venturi +2 more
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Nature, 1960
Sakaguchi and Murao1 reported on the presence of an enzyme in the mycelium of Penicillium chrysogenum and Aspergillus oryzae which would split penicillin G (I) into phenylacetic acid (II) and ‘penicin’ (III) :
C A, CLARIDGE, A, GOUREVITCH, J, LEIN
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Sakaguchi and Murao1 reported on the presence of an enzyme in the mycelium of Penicillium chrysogenum and Aspergillus oryzae which would split penicillin G (I) into phenylacetic acid (II) and ‘penicin’ (III) :
C A, CLARIDGE, A, GOUREVITCH, J, LEIN
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Phenylalkylsulfonyl Derivatives as Covalent Inhibitors of Penicillin Amidase
Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1984It was demonstrated that phenylmethanesulfonyl fluoride-a very potent inhibitor of penicillin amidase from Escherichia coli-binds covalently to the enzyme in molar ratio 1:1. The chloride, the azide and the N-hydroxysuccinimide ester of phenylmethanesulfonic acid are also very strong inactivators of the amidase.
M, Siewiński, M, Kuropatwa, A, Szewczuk
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Properties of penicillin amidase immobilized by copolymerization with acrylamide
Biotechnology and Bioengineering, 1979AbstractAn enzyme preparation in a spherical granule form was obtained by copolymerization of penicillin amidase (EC 3.5.1.11) (previously modified with maleic anhydride) and acrylamide via a crosslinking agent. As compared with the native enyme, immobilized amidase is more resistant to heating, has a lower affinity to benzylpenicillin, and is less ...
A, Szewczuk +4 more
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The role of penicillin amidases in nature and in industry
Trends in Biochemical Sciences, 1991Penicillin amidase (PA) is the enzyme used commercially for the production of semisynthetic penicillins. During the past decade, a detailed picture of the structure and regulation of the gene encoding this enzyme has emerged, revealing a variety of interesting features that are unique among microorganisms.
F, Valle +3 more
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