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  • 1
    Electronic Resource
    Electronic Resource
    Biosynthesis of penicillin V acylase by Fusarium sp.: effect of culture conditions (1993)
    Springer
    World journal of microbiology and biotechnology 9 (1993), S. 233-239 
    Details
    ISSN: 1573-0972
    Keywords: 6-Aminopenicillanic acid ; Fusarium sp. ; penicillin acylase ; penicillin V acylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Penicillin V acylase was produced, both intracellularly and extracellularly, by Fusarium sp. SKF 235 grown in submerged fermentation. When neopeptone was added to the medium, 〉95% of the penicillin V acylase was extracellular. In the absence of a complex organic nitrogen source, the fungus produced low levels of totally intracellular penicillin V acylase. MgSO4 was essential for synthesis of the enzyme, which was induced by phenoxyacetic acid and penicillin V. The maximum yield of penicillin V acylase was 430 IU/g dry cell wt. The optimum pH value and temperature for the penicillin V acylase were 6.5 and 55°C, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00327845
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  • 2
    Electronic Resource
    Electronic Resource
    Enzymatic splitting of penicillin V for the production of 6-APA using immobilized penicillin V acylase (1993)
    Springer
    World journal of microbiology and biotechnology 9 (1993), S. 630-634 
    Details
    ISSN: 1573-0972
    Keywords: 6-Aminopenicillanic acid ; Fusarium sp. ; immobilized enzyme ; penicillin acylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Penicillin V acylase from Fusarium sp. SKF 235 was immobilized on several cation-exchange resins, of which Amberlite CG-50 was preferred. Maximum activity of the immobilized penicillin V acylase was 250 to 280 IU/g dry beads. The pH and temperature optima of the enzyme shifted from 6.5 to 6.8 and 55°C to 60°C, respectively, as a result of immobilization. However, the K m for penicillin V remained at 10mm. Parameters for producing 6-aminopenicillanic acid were investigated and the immobilized penicillin V acylase was used for 68 cycles in a stirred tank reactor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00369569
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  • 3
    Electronic Resource
    Electronic Resource
    Production of 6-APA using a recirculated packed bed batch reactor (1992)
    Springer
    Biotechnology letters 14 (1992), S. 913-918 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A recirculated packed bed batch reactor has been designed for the production of 6-aminopenicillanic acid. It was observed that the flow rate of penicillin G solution is a rate limiting step for its hydrolysis. Under the conditions used, the maximum rate of hydrolysis of penicillin G was observed at a flow rate of 3.0 L/min.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01020628
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  • 4
    Electronic Resource
    Electronic Resource
    Immobilization of penicillin G acylase onto alumina: Effect of hydrophilicity (1991)
    Springer
    Biotechnology techniques 5 (1991), S. 401-404 
    Details
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Immobilization of penicillin G acylase was investigated on porous alumina and alumina treated with polyethyleneimine. The latter treatment increased the percent expression by 63 % and decreased the adsorption by 40 % indicating a crucial role of the hydrophobicity of alumina in adsorption and catalysis by, adsorbed penicillin G acylase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00185023
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  • 5
    Electronic Resource
    Electronic Resource
    Cephalosporin C acylase and penicillin V acylase formation by Aeromonas sp. ACY 95 (1996)
    Springer
    World journal of microbiology and biotechnology 12 (1996), S. 373-378 
    Details
    ISSN: 1573-0972
    Keywords: Aeromonas sp. ; 6-Aminopenicillanic acid ; 7-Aminocephalosporanic acid ; Cephalosporin C acylase ; Penicillin V acylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Aeromonas sp. ACY 95 produces constitutively and intracellularly a penicillin V acylase at an early stage of fermentation (12 h) and a cephalosporin C acylase at a later stage (36 h). Some penicillins, cephalosporin C and their side chain moieties/analogues, phenoxyacetic acid, penicillin V and penicillin G, enhanced penicillin V acylase production while none of the test compounds affected cephalosporin C acylase production. Supplementation of the medium with some sugars and sugar derivatives repressed enzyme production to varying degrees. The studies on enzyme formation, induction and repression, and substrate profile suggest that the cephalosporin C acylase and penicillin V acylase are two distinct enzymes. Substrate specificity studies indicate that the Aeromonas sp. ACY 95 produces a true cephalosporin C acylase which unlike the enzymes reported hitherto hydrolyses cephalosporin C specifically.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00340214
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  • 6
    Electronic Resource
    Electronic Resource
    Molecular biology of β-lactam acylases (1994)
    Springer
    World journal of microbiology and biotechnology 10 (1994), S. 129-138 
    Details
    ISSN: 1573-0972
    Keywords: Cephalosporin acylase ; glutaryl-7-ACA acylase ; penicillin G acylase ; penicillin V acylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract β-Lactam acylases such as penicillin G acylases, penicillin V acylases and glutaryl 7-aminocephalosporanic acid acylases are used in the manufacture of 6-aminopenicillanic acid, 7-aminodesacetoxycephalosporanic acid and 7-aminocephalosporanic acid (7-ACA). Genetically-engineered strains producing 1050 U/g, 3200 U/g and 7000 to 10,000 U/I of penicillin G acylase, penicillin V acylase and glutaryl-7-ACA acylase, respectively, have been developed. The penicillin G acylase studied to date and the glutaryl-7-ACA acylase from Pseudomonas sp. share some common features: the active enzyme molecules are composed of two dissimilar subunits that are generated from respective precursor polypeptide; the proteolytic processing is a post-translational modification which is regulated by temperature; and the Ser residue at the N-terminus of the β-sub-unit (Ser290; penicillin G acylase numbering) is implicated as the active site residue. Protein engineering, to generate penicillin G acylase molecules and their precursors with altered sequences, and the structure-function correlation of the engineered molecules are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00360873
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  • 7
    Electronic Resource
    Electronic Resource
    Effect of microenvironment of oxirane groups on the immobilization of penicillin G acylase (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 45 (1992), S. 279-284 
    Details
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Macroporous beaded terpolymers containing oxirane groups were synthesized for immobilization of penicillin G acylase. The effect of incorporation of various monomers such as hydroxyethyl methacrylate and methyl methacrylate, and the effect of crosslinking agents such as ethylene glycol dimethacrylate and divinyl benzene on binding and expression of penicillin G acylase were studied. The terpolymers were modified to varying extents by treating with polyethyleneimine. The influence of the microenvironment around the oxirane group on the binding and expression of penicillin G acylase was investigated.
    Additional Material: 7 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1992.070450209
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