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  • Mucuna pruriens L.  (2)
  • bioconversions  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Continuous production of the pharmaceutical 7,8-dihydroxy N-di-n-propyl 2-aminotetralin using a phenoloxidase from cell cultures of Mucuna pruriens (1990)
    Springer
    Plant cell, tissue and organ culture 23 (1990), S. 209-215 
    Details
    ISSN: 1573-5044
    Keywords: 2-aminotetralins ; bioconversion ; catechols ; continuous production ; Mucuna pruriens L. ; phenoloxidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Alginate-entrapped cells of Mucuna pruriens as well as the phenoloxidase isolated from the cell cultures, are able to ortho-hydroxylate several mono-, bi- and tri-cyclic monophenols. In this study, 7,8-dihydroxy N-di-n-propyl 2-aminotetralin, a catechol of pharmaceutical interest and difficult to prepare chemically, could be produced in considerable quantities by bioconversion of the precursor 7-hydroxy N-di-n-propyl 2-aminotetralin. A continuous flow system on a laboratory scale was used, which consisted of a phenoloxidase suspension in dialysis tubing as the biocatalysator in an airlift fermentor coupled with an aluminium oxide column for selective product isolation. Product formation continued for at least 50 h, resulting in ca. 130 mg product per liter, this being a bioconversion percentage of 25%. When the enzyme preparation was reused, 85% of the original activity was measured.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00034434
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  • 2
    Electronic Resource
    Electronic Resource
    Bioconversion of para-substituted monophenolic compounds into corresponding catechols by alginate entrapped cells ofMucuna pruriens (1988)
    Springer
    Plant cell, tissue and organ culture 13 (1988), S. 15-26 
    Details
    ISSN: 1573-5044
    Keywords: Mucuna pruriens ; entrapped plant cells ; bioconversions ; catechols ; isolation ; mass spectrometry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Alginate-entrapped cells ofM. pruriens were able to convert a number of parasubstituted monophenolic compounds into the corresponding catechols. All catechols produced were released into the medium, which offered the opportunity to isolate these products via a relatively simple procedure. Prepurification was performed on a Sephadex G10 gel and catechols were concentrated on Affigel 601. The identity of all products was confirmed with combined liquid chromatography/mass spectrometry (LC/MS) or MS using the desorption chemical ionization technique, depending on the catechol. For the entrapped cells and for a cell homogenate prepared of the same cell line ofM. pruriens the substrate specificities were qualitatively identical when judged on initial rates of synthesis calculated on protein basis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00043043
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  • 3
    Electronic Resource
    Electronic Resource
    Bioconversion of bi- and tri-cyclic monophenols by alginate-entrapped cells of Mucuna pruriens L. and by the partially purified Mucuna-phenoloxidase (1990)
    Springer
    Plant cell, tissue and organ culture 21 (1990), S. 9-15 
    Details
    ISSN: 1573-5044
    Keywords: 3-aminotetralins ; bioconversions ; catechols ; entrapped plant cells ; mass spectrometry ; Mucuna pruriens L.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Although alginate-entrapped cells of Mucuna pruriens L. possess a low substrate specificity, only para-substituted monocyclic phenols have been ortho-hydroxylated into catechols so far. In this study, compounds with more complex chemical structures were found to be substrates using entrapped cells of M. pruriens as well as the partially purified Mucuna-phenoloxidase. Thus, 5-, 6- and 7-hydroxylated 2-aminotetralins and a tricyclic compound, 9-hydroxy N-n-propyl hexahydronaphthoxazine, were converted into catechols. After isolation using preparative HPLC, the identity of the products was confirmed by MS. In general, for the entrapped cells and the enzyme preparation identical substrate specificities were found.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00034485
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