ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

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
Filter
  • Springer  (24)
  • 1
    Electronic Resource
    Electronic Resource
    Characterization of Gluconobacter oxydans immobilized in calcium alginate (1985)
    Springer
    Applied microbiology and biotechnology 22 (1985), S. 1-7 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Gluconobacter oxydans cells were immobilized in calcium alginate and the preparation was used for the oxidation of glycerol to dihydroxyacetone. The characterization was done according to the guidelines given by the Working Party on Immobilized Biocatalysts of the European Federation of Biotechnology. The pH optimum of the preparation was found to be 5.0 and the temperature optimum was 40°C. However, the operational stability was better at 30°C. The glycerol concentration required to obtain half the maximal reaction rate was about 5 mM for both immobilized and free cells. At low concentrations of glycerol and high concentrations of dihydroxyacetone a slight inhibition was noted. No loss of activity of the immobilized preparation was observed after storage for 68 days at +4°C. Investigation of the operational stability revealed a half-life of 5 days. Studies of the influence of particle size and cell densities as well as that of oxygen concentration revealed that the oxygen supply was the rate limiting step.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00252148
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Organic solvents for bioorganic synthesis (1987)
    Springer
    Applied microbiology and biotechnology 26 (1987), S. 1-8 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The influence of solvents on enzymatic activity and stability was investigated. As a model reaction the α-chymotrypsin-catalyzed esterification of N-acetyl-l-phenylalanine with ethanol was used. The enzyme was adsorbed on porous glass beads and used in various solvents. Small amounts of water were added to increase the enzymatic activity. These enzyme preparations obeyed. Michaelis-Menten kinetics. K m,app decreased slightly with the log P value of the solvent while V app increased markedly with the log P value. Log P values were also useful for generalizing the influence of solvents on enzyme stability. The enzyme preparations showed a markedly higher thermostability in dry solvents having log P values 〉0.7 than in less hydrophobic solvents. Also the operational stability was better in the more hydrophobic solvents. The amount of water added to the enzyme preparations greatly influenced the initial reaction rates. For some solvents optimal water contents were determined. The thermostability decreased with increasing water content. The observations are summarized in the conclusion that more hydrophobic solvents are preferable to less hydrophobic ones. The log P value gives a good guidance when selecting an organic solvent for enzymatic conversions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00282141
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Influence of the reaction medium on the product distribution of peroxidase-catalysed oxidation of p-cresol (1990)
    Springer
    Applied microbiology and biotechnology 33 (1990), S. 455-458 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary p-Cresol was oxidized by hydrogen peroxide in a reaction catalysed by horseradish peroxidase and the low molecular weight products were investigated. In aqueous media Pummerer's ketone (I) was the dominating product but in organic media the product distribution was quite different; 2,2'-dihydroxy-5,5'-dimethyldiphenyl (II) was the main low molecular weight product. Similar product distributions were obtained with peroxidase adsorbed on a solid support and suspended in toluene and with peroxidase solubilized in a microemulsion containing the same solvent. The best selectivity for the formation of (II) was obtained when the enzyme was adsorbed on Celite and suspended in water-saturated chloroform with 0.5% (v/v) extra water added. The yield of low molecular weight products in this case was 28%; of this fraction, 95% was (II).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00176665
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Oxygen supply to immobilized cells (1982)
    Springer
    Applied microbiology and biotechnology 16 (1982), S. 165-170 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Oxygen supply is a critical point in technical processes when aerobic cells are used in immobilized preparations. This report concerns the use of hemoglobin or emulsions of perfluorochemicals (completely fluorinated organic compounds) to carry oxygen to immobilized cells. Both methods work well and do not seem to harm the cells. The perfluorochemical method of improving oxygen supply showed a higher operational stability than the hemoglobin method.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00505826
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Activity and operational stability of immobilized mandelonitrile lyase in methanol/water mixtures (1988)
    Springer
    Applied microbiology and biotechnology 29 (1988), S. 419-425 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The enzyme mandelonitrile lyase was covalently immobilized on solid support materials using different methods. Immobilization on porous silica using coupling with glutaraldehyde afforded preparations with high enzyme loading (up to 9% (w/w)). The immobilized enzyme was used in a packed bed reactor for the continuous production of d-mandelonitrile from benzaldehyde and cyanide. The influence of the flow rate, pH, substrate concentrations and enzyme loading on the reaction yield and the enantiomeric purity of the product was investigated. In order to suppress the competing spontaneous reaction, the enzymatic reaction must be rapid. A flow rate of 9.5 ml/min (0.1 M benzaldehyde and 0.3 M HCN) through a 3 ml reactor afforded a 86% yield of mandelonitrile with 92% enantiomeric excess. No leakage of enzyme occurred under continuous operation. One column was used continuously for 200 h without any decrease in yield or enantiomeric purity of the product. High concentrations of benzoic acid were shown to decrease the operational stability of the system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00269062
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Oxidation of trans- and cis-1,2-cyclohexanediol by Gluconobacter oxydans (1989)
    Springer
    Applied microbiology and biotechnology 30 (1989), S. 257-263 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The enzymatic oxidation of 1,2-cyclohexanediol and related substrates by Gluconobacter oxydans (ATCC 621) was investigated. At low pH, membrane-bound enzymes were active and at high pH, NAD-dependent, soluble enzymes showed activity. Whole bacterial cells were used to catalyze some bioconversions. Racemic trans-1,2-cyclohexanediol was oxidized at pH 3.5 to give (R)-2-hydroxycyclohexanone (96% e.e.) and at pH 8.0 the same substrate was oxidized to (S)-2-hydroxycyclohexanone (97% e.e.). The latter conversion was severely inhibited by the reaction product while the former was not significantly product inhibited. (S)-2-hydroxycyclohexanone (97% e.e.) was also prepared from cis-1,2-cyclohexanediol by oxidation with G. oxydans cells at pH 3.5 in a reaction which continued to 100% conversion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00256215
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Interesterification of phosphatidylcholine with lipases in organic media (1990)
    Springer
    Applied microbiology and biotechnology 33 (1990), S. 255-258 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Lipases were investigated with respect to their ability to catalyse the incorporation of fatty acids into phosphatidylcholine (PC) by interesterification reactions. The enzymes were dried onto solid support materials and the conversions were carried out in water-saturated toluene. Three lipases (two fungal and one plant enzyme) had the desired activity; immobilized lipase from Mucor miehei (Lipozyme) was the most active enzyme. The Lipozyme-catalysed interesterification was selective for the sn-1 position of PC and during 48 h of reaction around 50% of the fatty acids in this position were replaced with heptadecanoic acid, a fatty acid which was practically absent in the original phospholipid. Due to adsorption on the support material and the competing hydrolysis reaction the total amount of PC in the reaction solution decreased to about 40% of the original amount. Higher interesterification rates were obtained with free fatty acids as acyl donors than with fatty acid esters.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00164517
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Oxygen supply to immobilized cells (1984)
    Springer
    Applied microbiology and biotechnology 20 (1984), S. 296-302 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Oxygen supply is a critical point in technical processes when aerobic cells are used in immobilized preparations. In this study p-benzoquinone is used as a substitute for oxygen in the oxidation of glycerol to dihydroxyacetone by immobilized Gluconobacter oxydans cells. The reaction rate was much higher when p-benzoquinone was used compared to when oxygen was used. In an experiment with free cells p-benzoquinone gave a rate more than four times that of oxygen, and with immobilized cells the difference was even greater. p-benzoquinone is more effective than oxygen because it gives a higher maximal reaction rate (the reason for this fact is discussed) and because it is more soluble in water than oxygen. The operational stability of the process is comparatively good. In one experiment the productivity decreased from 60 to 10 mmol/h·g over an 8-day period when p-benzoquinone was used. When oxygen was used in a similar experiment the productivity decreased from 14 to 6 mmol/h·g. The byproduct formed from p-benzoquinone, hydroquinone, can be oxidized to p-benzoquinone which can be re-used. Seven succesive regenerations of p-benzoquinone were performed without any loss of efficiency.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00270589
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    facet.materialart.
    Unknown
    Characterization of Gluconobacter oxydans immobilized in calcium alginate (1985)
    Springer
    Details
    Publication Date: 1985-05-01
    Print ISSN: 0175-7598
    Electronic ISSN: 1432-0614
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Springer
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 10
    facet.materialart.
    Unknown
    Xylo- and arabinoxylooligosaccharides from wheat bran by endoxylanases, utilisation by probiotic bacteria, and structural studies of the enzymes (2018)
    Springer
    Details
    Publication Date: 2018-02-14
    Print ISSN: 0175-7598
    Electronic ISSN: 1432-0614
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Springer
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...