Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    An in vivo analysis of the energetics of aldose oxidation by Acinetobacter calcoaceticus (1987)
    Springer
    Applied microbiology and biotechnology 26 (1987), S. 560-567 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A continuous culture study was made of the energetics of oxidation of various aldose sugars by Acinetobacter calcoaceticus LMD 79.41. The consumption of aldoses during carbon- and energy-limited growth of the organism on mixtures of acetate and an aldose was independent of the pH of the culture. Acid production, however, was strongly dependent on this parameter. It is shown that aldose consumption without concurrent acid production is due to formation of the corresponding lactone, the hydrolysis of which is pH-dependent. The cell yield of A. calcoaceticus on mixtures of acetate and glucose or xylose was much higher than during growth on acetate alone. This increase in cell yield was, however, dependent on the pH of the culture. Only at pH values which permitted a high rate of lactone hydrolysis an enhancement of the cell yield was observed. These results suggest that lactone hydrolysis has an important bearing on the efficiency of periplasmic oxidation of aldoses in bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00253033
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Effect of various co-substrates on 1,2-epoxypropane formation from propene by ethene-utilizing Mycobacteria (1987)
    Springer
    Applied microbiology and biotechnology 26 (1987), S. 434-438 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Ethanol, ethylacetate and ethene were tested as no-substrates to improve prolonged 1,2-epoxypropane formation from propene by immobilized cells of three strains (Eu1, 2W, E3) of ethene-utilizing Mycobacteria. Cells grown either on ethene or on both ethene and ethanol were immobilised on lava and the effect of co-substrates on 1,2-epoxypropane formation from propene was recorded in a gas/solid bioreactor. The rate of 1,2-epoxypropane formation by immobilized cells of strains Eu1 and 2W was significantly enhanced when ethanol or ethylacetate were supplied simultaneously with propene, while biocatalysis during a prolonged period of time was achieved in the presence of ethylacetate. Co-substrates had no beneficial effect on 1,2-epoxypropane formation by strain E3. It was possible to increase the 1,2-epoxypropane formation rate by immobilized cells over a period of three weeks of operation by supplying propene and ethene alternately.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00253527
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Inactivation of alkene oxidation by epoxides in alkene-and alkane-grown bacteria (1985)
    Springer
    Applied microbiology and biotechnology 22 (1985), S. 428-433 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The oxidation of propene by resting-cells of ethene-grown Mycobacterium E3 was inactivated by 1,2-epoxypropane. Inactivation increased with increasing epoxide concentrations with 50% inactivation at approximately 30 mM epoxide. Other lower epoxides as epoxyethane and 1,2-epoxybutane also inactivated oxidation of propene as well as of other alkenes. Propene oxidation by resting-cells of ethane-grown Mycobacterium E20 and resting-cells of methane-grown Methylosinus trichosporium OB3b was inactivated for 50% at much lower 1,2-epoxypropane concentrations of approximately 1 and 3 mM respectively. It was demonstrated that in vivo the predominant effect of 1,2-epoxypropane was on the epoxidizing enzyme, i.e. alkene mono-oxygenase (strain E3), alkane mono-oxygenase (strain E20) and methane mono-oxygenase (methylotroph) and that the effect of the epoxide on the alkene mono-oxygenase was irreversible.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00252785
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Bioformation of 4-hydroxybenzoate from 4-chlorobenzoate by Alcaligenes denitrificans NTB-1 (1986)
    Springer
    Applied microbiology and biotechnology 25 (1986), S. 289-294 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Strain NTB-1, identified as a Alcaligenes denitrificans sp., was isolated from a mixture of soil and sewage samples using 4-chlorobenzoate as sole carbon and energy source. Simultaneous adaptation experiments and enzyme studies revealed that 4-chlorobenzoate was converted to 4-hydroxybenzoate which was further oxidized yielding 3,4-dihydroxybenzoate. Bioformation of 4-hydroxybenzoate from 4-chlorobenzoate when 4-chlorobenzoate-grown cells were incubated with 4-chlorobenzoate under conditions of low and controlled oxygen concentrations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00253665
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    The involvement of an enantioselective transaminase in the metabolism of D-3- and D-4-hydroxyphenylglycine inPseudomonas putida LW-4 (1988)
    Springer
    Applied microbiology and biotechnology 29 (1988), S. 224-230 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Pseudomonas putida LW-4, isolated on D-phenylglycine as sole carbon and energy source, was also able to grow on D-3-and D-4-hydroxyphenylglycine. Both D-3-and D-4-hydroxyphenylglycine were initially converted to the corresponding hydroxyphenylglyoxylates by means of an enantioselective transaminase. Subsequently, the hydroxyphenylglyoxylates were decarboxylated and then oxidized to 3-and 4-hydroxybenzoate, respectively. These latter compounds in turn were oxidized by NADPH-dependent hydroxylases to protocatechuate, which was further oxidized via an intradiol cleavage. Preliminary experiments with cell extracts in which the 4-hydroxyphenylglyoxylate decarboxylase was partially removed by an ammonium sulfate fractionation showed that D-4-hydroxyphenylglyoxycine could be formed from 4-hydroxyphenylglyoxylate by the enantioselective transaminase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01982906
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Chiral resolution of 2,3-epoxyalkanes by Xanthobacter Py2 (1988)
    Springer
    Applied microbiology and biotechnology 27 (1988), S. 337-340 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary With propene-grown cells of Xanthobacter Py2 it was possible to resolve racemic mixtures of 2,3-epoxyalkanes. Only 2S-forms were metabolized by this organism, resulting in pure 2R-2,3-epoxyalkanes. Chiral resolution was obtained with trans-2,3-epoxybutane, trans-2,3-epoxypentane and cis-2,3-epoxypentane. Xanthobacter Py2 was however not able to discriminate between the enantiomeric forms of 1,2-epoxyalkanes, resulting in the complete degradation of both chiral forms of 1,2-epoxyalkanes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00251764
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    The involvement of an enantioselective transaminase in the metabolism of D-3- and D-4-hydroxyphenylglycine inPseudomonas putida LW-4 (1988)
    Springer
    Applied microbiology and biotechnology 29 (1988), S. 224-230 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Pseudomonas putida LW-4, isolated on D-phenylglycine as sole carbon and energy source, was also able to grow on D-3-and D-4-hydroxyphenylglycine. Both D-3-and D-4-hydroxyphenylglycine were initially converted to the corresponding hydroxyphenylglyoxylates by means of an enantioselective transaminase. Subsequently, the hydroxyphenylglyoxylates were decarboxylated and then oxidized to 3-and 4-hydroxybenzoate, respectively. These latter compounds in turn were oxidized by NADPH-dependent hydroxylases to protocatechuate, which was further oxidized via an intradiol cleavage. Preliminary experiments with cell extracts in which the 4-hydroxyphenylglyoxylate decarboxylase was partially removed by an ammonium sulfate fractionation showed that D-4-hydroxyphenylglyoxycine could be formed from 4-hydroxyphenylglyoxylate by the enantioselective transaminase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00939311
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Epoxidation of alkenes by alkene-grown Xanthobacter spp. (1986)
    Springer
    Applied microbiology and biotechnology 24 (1986), S. 334-337 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Newly isolated Xanthobacter spp. were able to grow on the gaseous alkenes like ethene, propene, 1-butene and 1,3-butadiene. Resting-cell suspensions of propene-, 1-butene- or 1,3-butadiene-grown Xanthobacter Py10 accumulated 1,2-epoxyethane from ethene. Ethene-grown Xanthobacter Py10 did not produce any 1,2-epoxyalkane from the alkenes tested. Furthermore, propenegrown Xanthobacter Py2 accumulated 2,3-epoxybutane from trans-butene and cis-butene but did not form epoxides from other substrates tested.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00257059
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Microbial metabolism of d- and l-phenylglycine by Pseudomonas putida LW-4 (1986)
    Springer
    Archives of microbiology 144 (1986), S. 169-174 
    Details
    ISSN: 1432-072X
    Keywords: Phenylglycine degradation ; Transamination of d- and l-phenylglycine ; Pseudomonas putida
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A strain of Pseudomonas putida capable of utilizing both stereoisomers of phenylglycine as the sole carbon and energy source was isolated from soil. No phenylglycine racemase was detected in cells grown on either stereoisomer. In an initial reaction each steroisomer of phenylglycine was transaminated yielding phenylglyoxylate which was further metabolized via benzaldehyde to benzoate. Subsequently, benzoate was further degraded via an ortho-cleavage of catechol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414730
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Catabolism of dl-α-phenylhydracrylic, phenylacetic and 3- and 4-hydroxyphenylacetic acid via homogentisic acid in a Flavobacterium sp. (1988)
    Springer
    Archives of microbiology 149 (1988), S. 207-213 
    Details
    ISSN: 1432-072X
    Keywords: dl-α-Phenylhydracrylic acid ; Phenylacetic acid ; Flavobacterium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A degradation pathway for dl-α-phenylhydracrylic, phenylacetic, 3- and 4-hydroxyphenylacetic acid by a Flavobacterium is presented. Experiments with washed cells and enzyme studies revealed that dl-α-phenylhydracrylic acid in an initial reaction was oxidatively decarboxylated to phenylacetaldehyde. Whole cells oxidized both stereoisomers of phenylhydracrylic acid at different rates. The product phenylacetaldehyde in turn was oxidized to phenylacetic acid. No hydroxylation of phenylacetic acid was detected in cell extracts, but on the basis of experiments with washed cells it is assumed that phenylacetic acid is mainly metabolized via 3-hydroxyphenylacetic acid. This latter product was subsequently hydroxylated yielding the ring-cleavage substrate homogentisate. 4-Hydroxyphenylacetic acid was also degraded via homogentisate. Ringcleavage of homogentisate gave maleylacetoacetate which was further degraded through a glutathione-dependent pathway. Homoprotocatechuate was not an intermediate in the metabolism of dl-phenylhydracrylic acid, phenylacetic, 3- and 4-hydroxyphenylacetic acid metabolism, but it could be hydroxylated aspecifically to 2,4,5-trihydroxyphenylacetic acid by the action of the 3-hydroxyphenylacetic acid-6-hydroxylase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00422006
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...