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  • 1
    ISSN: 0168-1656
    Keywords: Amidase ; Enantioselective enzyme ; Naproxen ; Nitrile ; Nitrile hydratase ; Rhodococcus
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 47 (1997), S. 668-674 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A series of enrichments with different nitriles as sole source of nitrogen was performed in order to obtain a relationship between the selective nitrogen source and (i) the enzyme systems that are synthesized by the isolates and (ii) the enzyme specificities for the utilization of the nitriles. Bacteria were enriched with 2-phenylpropionitrile, 2-(2-methoxyphenyl)propionitrile, 2-phenylbutyronitrile, ibuprofen nitrile, naproxen nitrile, ketoprofen nitrile, ketoprofen amide, benzonitrile, or naphthalenecarbonitrile as sole nitrogen source and succinate as sole source of carbon and energy. 2-Phenylpropionitrile as nitrogen source resulted predominantly in the enrichment of gram-negative bacteria, which harboured nitrilase and in some cases also amidase activity. In contrast, with the other nitriles used, a substantial majority of gram-positive strains, mainly of the genus Rhodococcus, were isolated. These strains contained predominantly a nitrile hydratase/amidase system. The nitrilases and nitrile hydratases showed R or S selectivity with generally poor optical yields. In contrast, the amidases were almost exclusively S-selective, often forming the optically pure acids with an enantiomeric excess above 99%. The conversion of different nitriles by the isolates was compared. The nitrile-hydrolysing systems of the new isolates usually showed high activity against those nitriles that were used for the enrichment of the bacteria.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Bacteria were enriched from soil samples with succinate as carbon source and racemic 2-phenylpropionitrile as sole source of nitrogen. One of the isolates, strain d3, converted (R,S)-2-phenylpropionitrile with high enantioselectivity to (S)-2-phenylpropionic acid. Strain d3 was identified as Agrobacterium tumefaciens. Resting cells hydrolysed 2-phenylpropionitrile via 2-phenylpropionamide to 2-phenylpropionic acid. Racemic 2-phenylpropionitrile as well as 2-phenylpropionamide were converted to (S)-2-phenylpropionic acid with an enantiometric excess above 96%. The nitrile hydratase and the amidase were both shown to convert preferentially the S enantiomer of their respective substrate. These two enzymes were induced in the presence of (R,S)-2-phenylpropionitrile but only in the absence of ammonia. In addition to 2-phenylpropionitrile strain d3 could utilize various aliphatic and aromatic nitriles as nitrogen sources. Resting cells of strain d3 also converted (R,S)-2-phenylbutyronitrile, ibuprofen nitrile, ketoprofen nitrile and α-aminophenylacetonitrile with high enantioselectivity. The nitrile- and amide-converting enzyme activities were also found in cell-free extracts.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Bacteria were enriched from soil samples with succinate as carbon source and racemic 2-phenylpropionitrile as sole source of nitrogen. One of the isolates, strain d3, converted (R,S)-2-phenylpropionitrile with high enantioselectivity to (S)–2-phenylpropionic acid. Strain d3 was identified as Agrobacterium tumefaciens. Resting cells hydrolysed 2-phenylpropionitrile via 2-phenylpropionamide to 2-phenylpropionic acid. Racemic 2-phenylpropionitrile as well as 2-phenylpropionamide were converted to (S)-2-phenylpropionic acid with an enantiomeric excess above 96%. The nitrile hydratase and the amidase were both shown to convert preferentially the S enantiomer of their respective substrate. These two enzymes were induced in the presence of (R,S)-2-phenylpropionitrile but only in the absence of ammonia. In addition to 2-phenylpropionitrile strain d3 could utilize various aliphatic and aromatic nitriles as nitrogen sources. Resting cells of strain d3 also converted (R,S)-2-phenylbutyronitrile, ibuprofen nitrile, ketoprofen nitrile and α-aminophenylacetonitrile with high enantioselectivity. The nitrile- and amide-converting enzyme activities were also found in cell-free extracts.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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