Library

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
    s.l. : American Chemical Society
    Biotechnology progress 8 (1992), S. 291-297 
    ISSN: 1520-6033
    Source: ACS Legacy Archives
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 672 (1992), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biotechnology progress 10 (1994), S. 403-409 
    ISSN: 1520-6033
    Source: ACS Legacy Archives
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 45 (1995), S. 536-538 
    ISSN: 0006-3592
    Keywords: chiral balance ; enantiomeric excess ; kinetic resolution ; diastereomers ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: When kinetic resolution is applied for the production of enantiomerically pure compounds, process options may be used which involve more than one chiral substrate and one chiral product, such as sequential or parallel enzymatic kinetic resolutions or hydrolysis of diastereomers. Although the relation between the yields (y) of the chiral compounds is straightforward in these cases, the relation between their enantiomeric excess (ee) values is not. Combining mass balances into a so-called chiral balance (Σ y · eeR = 0) provides the relation between enantiomeric excess values in a useful manner. This chiral balance easily shows which nonmeasured enantiomeric excess values and yields can be calculated from measured values. The chiral balance is only valid when configurations at chiral centers are conserved. © 1995 John Wiley & Sons, Inc.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 43 (1994), S. 411-422 
    ISSN: 0006-3592
    Keywords: enzyme kinetics ; progress curve ; enantioselectivity ; covariance ; kinetic resolution ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The present study deals with kinetic modeling of enzyme-catalyzed reactions by integral progress curve analysis, and shows how to apply this technique to kinetic resolution of enantiomers. It is shown that kinetic parameters for both enantiomers and the enantioselectivity of the enzyme may be obtained from the progress curve measurement of a racemate only.A parameter estimation procedure has been established and it is shown that the covariance matrix of the obtained parameters is a useful statistical tool in the selection and verification of the model structure. Standard deviations calculated from this matrix have shown that progress curve analysis yields parameter values with high accuracies.Potential sources of systematic errors in (multiple) progress curve analysis are addressed in this article. Amongst these, the following needed to be dealt with: (1) the true initial substrate concentrations were obtained from the final amount of product experimentally measured (mass balancing); (2) systematic errors in the initial enzyme concentration were corrected by incorporating this variable in the fitting procedure as an extra parameter per curve; and (3) enzyme inactivation is included in the model and a first-order inactivation constant is determined.Experimental verification was carried out by continuous monitoring of the hydrolysis of ethyl 2-chloropropionate by carboxylesterase NP and the α-chymotrypsin-catalyzed hydrolysis of benzoylalanine mathyl ester in a pH-stat system. Kinetic parameter values were obtained with high accuracies and model predictions were in good agreement with independent measurements of enantiomeric excess values or literature data. © 1994 John Wiley & Sons, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...