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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 750 (1995), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 613 (1990), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 40 (1994), S. 599-605 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract. In an extended screening using d,l-carnitine amide as carbon or nitrogen source about 1300 strains were obtained by enrichment culture. Of these, 65 strains possessed carnitine amidase activities. A single strain was identified as containing an enzyme able to hydrolyse only l-carnitine amide and yield carnitine of high enantiomeric purity (≥97) when incubated with the racemic substrate. During the initial optimisation of the culture conditions the volume activity could be improved 6.7-fold whereas the specific activity increased 3.6-fold. The enzyme is inducible by l-carnitine amide and carnitine and to a lesser degree also by γ-butyrobetaine and dehydrocarnitine. As judged by the fatty acids and quinone composition the strain belongs into the α-subgroup of purple bacteria but has not yet been classified by the German Culture Collection into a known genus of bacteria.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 34 (1991), S. 604-607 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary 3-Hexulose phosphate synthase was purified in 94% yield from Methylomonas M15. The enzyme did not form a Schiff-base intermediate with d-ribulose 5-phosphate that could be reduced by NaBH4. However, the enzyme required Mg2+ or Mn2+ ions for activity and was inactivated in the presence of EDTA. The latter is a property of class II aldolases. The enzyme accepted a wide range of other aldehydes in addition to its natural substrate formaldehyde, while d-ribulose 5-phosphate could not be replaced. This makes it an attractive tool for the synthesis of higher sugar phosphates.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 38 (1992), S. 334-340 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract In a limited screening 65 microorganisms were tested with regard to their ability to reduce keto acids or esters of different chain length and position of the keto group with NADH or NADPH as coenzymes. Twenty-seven organisms exhibited reductase activity. Among these, Candida parapsilosis and Rhodococcus erythropolis have been chosen for further investigation. The keto ester reductases of both C. parapsilosis and R. erythropolis prefer NADH as coenzyme and show higher activity towards keto esters than keto acids. The keto ester reductase production of C. parapsilosis during growth passed a maximum in the late exponential phase, decreased and reaches a plateau in the stationary phase. In contrast, the specific activity of the keto ester reductase of R. erythropolis did not decrease in the stationary growth phase. The enzyme of C. parapsilosis was inducible by a keto ester when growing on glycerol as the sole carbon source. Furthermore, the enzyme of C. parapsilosis was subject to catabolite repression. When C. parapsilosis and R. erythropolis were cultivated on n-alcane the specific activity of their keto ester reductases was enhanced about seven- and eightfold, respectively, compared to growth on glucose. This leads to the assumption that, while growing on n-alcane, a degradation product is formed in both strains that induces the production of the keto ester reductase.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 40 (1994), S. 606-610 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract. A novel enzyme, l-carnitine amidase, was purified about 140-fold from a newly screened microorganism (DSM 6320) to yield a homogeneous protein. The native enzyme has a molecular mass of 125 kDa (gel filtration) and consists of two identical subunits as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and Edman degradation. The pH optimum was found around pH 8.5. Out of 60 chemicals tested as substrates (amides of various aliphatic and aromatic acids, nitriles, amino acid amides and dipeptide amides) the amidase hydrolysed only l-carnitine amide. The Michaelis constant (Km) was found to be 11.6 mm, and the pure protein had a specific activity of 328 units/mg. Complex kinetics were observed with the racemic mixture of d,l-carnitine amide as starting material during enzymatic hydrolysis.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 33 (1990), S. 324-329 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Several strains of Gram-negative microorganisms were screened for maximum 3-deoxy-d-manno-2-octulosonic acid (KDO) aldolase (EC 4.1.2.23) activity. Although this enzyme has been noted to be inducible on special medium, no induction was found. By centrifugation studies the KDO aldolase was found to be localized in the cell wall or membrane fraction. The enzyme activity was very susceptible to small amounts of detergent in solution.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 40 (1994), S. 599-605 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract In an extended screening using d,l-carnitine amide as carbon or nitrogen source about 1300 strains were obtained by enrichment culture. Of these, 65 strains possessed carnitine amidase activities. A single strain was identified as containing an enzyme able to hydrolyse only l-carnitine amide and yield carnitine of high enantiomeric purity (≥97) when incubated with the racemic substrate. During the initial optimisation of the culture conditions the volume activity could be improved 6.7-fold whereas the specific activity increased 3.6-fold. The enzyme is inducible by l-carnitine amide and carnitine and to a lesser degree also by λ-butyrobetaine and dehydrocarnitine. As judged by the fatty acids and quinone composition the strain belongs into the α-subgroup of purple bacteria but has not yet been classified by the German Culture Collection into a known genus of bacteria.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 40 (1994), S. 606-610 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A novel enzyme, l-carnitine amidase, was purified about 140-fold from a newly screened microorganism (DSM 6320) to yield a homogeneous protein. The native enzyme has a molecular mass of 125 kDa (gel filtration) and consists of two identical subunits as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and Edman degradation. The pH optimum was found around pH 8.5. Out of 60 chemicals tested as substrates (amides of various aliphatic and aromatic acids, nitriles, amino acid amides and dipeptide amides) the amidase hydrolysed only l-carnitine amide. The Michaelis constant (Km) was found to be 11.6 mm, and the pure protein had a specific activity of 328 units/mg. Complex kinetics were observed with the racemic mixture of d,l-carnitine amide as starting material during enzymatic hydrolysis.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Glycoconjugate journal 15 (1998), S. 139-145 
    ISSN: 1573-4986
    Keywords: activated deoxysugars ; preparative enzymatic synthesis ; sucrose synthase ; dehydratase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract dTDP–6–deoxy–4–keto–D–glucose (1), the common intermediate in the biosyntheses of the mainfold deoxysugars, was synthesized on a gram–scale by the combination of sucrose synthase and dTDP–D–glucose 4,6–dehydratase in a fed batch, starting the reaction with dTDP. This process allowed a dTDP conversion with a 100% rate. An easy and efficient three–step purification with anion–exchange chromatography and gel filtration gave 1.1 g of 1 in an overall yield of 73%. This work realizes a first step for an economic access to activated deoxysugars.
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