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
    Kinetic behaviour of penicillin acylase stabilized by poly (ethyleneimine) (1995)
    Springer
    Bioprocess and biosystems engineering 13 (1995), S. 183-187 
    Details
    ISSN: 1432-0797
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The paper presents the kinetic evaluations of poly(ethyleneimine)-penicillin acylase preparations. The comparative studies show that the investigated system is much better than the native enzyme, and slightly worse than commercially available Boenringer preparation. Additionally, the high stability of PEI-enzyme system, very easy way of its preparation, high flexibility, and possibility to set the needed enzyme concentration are particularly favourable for use of the membrane bioreactor with PEI-enzyme system immobilized in its volume. Some advantages of the use of such bioreactor are also discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00367252
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Immobilization of penicillin acylase on acrylic carriers (1989)
    Springer
    Bioprocess and biosystems engineering 4 (1989), S. 159-162 
    Details
    ISSN: 1432-0797
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Penicillin acylase obtained from E. Coli (E. C. 3.5.1.11) was covalently bound via glutaric aldehyde to acrylic carriers crosslinked with divinylbenzene or ethylene glycol dimethacrylate. The best enzymatic preparation was obtained by using ethyl acrylate/ ethylene glycol dimethacrylate copolymer. 1 cm3 of the carrier bound 6.4 mg of protein, having 72% activity in relation to the native enzyme. The preparation lost only 10% of its initial activity after 100 d of storage at 4°C. A negligible effect of immobilization on the enzyme activity at different temperatures or pH as well as significant increase of the stability of the immobilized enzyme at elevated temperatures were observed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00369394
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Kinetic behavior of penicillin acylase immobilized on acrylic carrier (1993)
    Springer
    Bioprocess and biosystems engineering 9 (1993), S. 37-42 
    Details
    ISSN: 1432-0797
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The usefulness of Lilly's kinetic equation to describe penicillin G hydrolysis performed by immobilized penicillin acylase onto the acrylic carrier has been shown. Based on the experimental results characteristic kinetic constants have been estimated. The effect of noncompetitive inhibition of 6-amino penicillanic acid has not been found. Five components of reaction resistance have been defined. These components were also estimated for the reaction of the native enzyme as well as the Boehringer preparation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00389538
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Process of penicillin G hydrolysis catalyzed by penicillin acylase immobilized on acylic carrier (1993)
    Springer
    Bioprocess and biosystems engineering 9 (1993), S. 271-275 
    Details
    ISSN: 1432-0797
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The usefulness of penicillin acylase immobilized onto butyl acrylate — ethyl glycol dimethacrylate (called in this paper acrylic carrier) in penicillin G hydrolysis performed in a stirred tank reactor is shown. The enzyme-acrylic carrier preparation does not deteriorate its own properties in the mixing condition of slurry reactor. The experiments were carried out in a batch and a continuous stirred tank reactor as well as continuous stirred tank reactors in series. It was found to be a satisfactory agreement between experimental and predicted results. It also indicated the optimal substrate concentration range which provides the most effective enzyme operation. A superiority of the three reactors in series over the batch reactor is shown.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01061533
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Storage stabilization and purification of enzyme by water-soluble synthetic polymers
    Amsterdam : Elsevier
    Enzyme and Microbial Technology 16 (1994), S. 616-621 
    Details
    ISSN: 0141-0229
    Keywords: Water-soluble polymers ; activity stabilization ; penicillin acylase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0141-0229(94)90128-7
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Kinetic behaviour of penicillin acylase stabilized by poly (ethyleneimine) (1995)
    Springer
    Bioprocess engineering 13 (1995), S. 183-187 
    Details
    ISSN: 0178-515X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  The paper presents the kinetic evaluations of poly(ethyleneimine)-penicillin acylase preparations. The comparative studies show that the investigated system is much better than the native enzyme, and slightly worse than commercially available Boenringer preparation. Additionally, the high stability of PEI-enzyme system, very easy way of its preparation, high flexibility, and possibility to set the needed enzyme concentration are particularly favourable for use of the membrane bioreactor with PEI-enzyme system immobilized in its volume. Some advantages of the use of such bioreactor are also discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00367252
    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...