Staff Publications

Staff Publications

  • external user (warningwarning)
  • Log in as
  • language uk
  • About

    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

    We have a manual that explains all the features 

Record number 404954
Title The use of L-lysine decarboxylase as a means to separate amino acids by electrodialysis
Author(s) Teng, Y.; Scott, E.L.; Zeeland, A.N.T. van; Sanders, J.P.M.
Source Green Chemistry 13 (2011)3. - ISSN 1463-9262 - p. 624 - 630.
Department(s) Biobased Chemistry and Technology
FBR BP Biorefinery & Natural Fibre Technology
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) nitrogen-containing chemicals - biobased production - enzyme electrode - bulk chemicals - immobilization - alginate - biomass
Abstract Amino acids (AA's) are interesting materials as feedstocks for the chemical industry as they contain chemical functionalities similar to conventional petrochemicals. This offers the possibility to circumvent process steps, energy and reagents. AA's can be obtained by the hydrolysis of potentially inexpensive voluminous protein streams derived from biofuel production. However, isolation of the preferred AA is required in order to carry out further transformation into the desired product. Theoretically separation may be achieved using electrodialysis. To increase efficiency, specific modification to a product of industrial interest and removes charged groups of AA's with similar isoelectric points is required. Here, the reaction of L-lysine decarboxylase (LDC) was studied as a means to specifically convert L-lysine (Lys) to 1,5-pentanediamine (PDA) in the presence of L-arginine (Arg) to produce products with different charge thus allowing isolation of products by electrodialysis. Immobilization of LDC in calcium alginate enhanced the operational stability and conversion in mixtures of amino acids was highly specific. At 30 °C the presence of Arg had little effect on the activity of the enzyme although inhibition by the product PDA could be observed. Volumetric productivity was calculated and raw material and transformation costs were estimated for a potential process using a mixture of Arg and Lys.
There are no comments yet. You can post the first one!
Post a comment
Please log in to use this service. Login as Wageningen University & Research user or guest user in upper right hand corner of this page.