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- Title
Amide-Bond Syntheses Catalyzed by Penicillin Acylase.
- Authors
Pessina, Antonio; Lüthi, Peter; Luisi, Pier Luigi; Prenosil, Jiri; Zhang, You-Shang
- Abstract
The enzymatic synthesis of amide bonds catalyzed by penicillin acylase is investigated both in H2O solution and in organic solvents containing reverse micelles. The specificity of the reaction is rather high on the side of the acyl component, practically only phenylacetic acid gives sizeable yields. On the contrary, a variety of amino-acid esters, dipeptides, and tripeptides can be used as amino component, e.g., serine methyl ester, methionine ethyl ester, tyrosine ethyl ester, Gly-Asp, Ala-Tyr, Gly-Tyr-Gly etc. However, Many other amino-acid residues do not react, and the possible reasons for this are discussed. Yields varyin rang the 10-80%. A. systematic study to optimize yields by varying the solvent composition is presented for one model reaction. The enzyme is also able to couple certain D-amino-acid residues (e.g. D-methionine ethyl ester or Gly- D-Asp) though at lower rate. Reverse micelles formed by the cationic surfactant cetyltrimethylammonium bromide (CTAB) in CHCl3/isooctane are used to host penicillin acylase and to perform amide synthesis in which the product is perferentially soluble in the organic solvent mixture. The reaction is studied as a function of pH and certain micellar parameters, e. g. wo (wo = [H2O]/[CTAB]). A new membrane enzyme reactor is utilized to separate the product from the enzyme-containing micelles. The adavantges and the limits of this approach are discussed.
- Publication
Helvetica Chimica Acta, 1988, Vol 71, Issue 3, p631
- ISSN
0018-019X
- Publication type
Article
- DOI
10.1002/hlca.19880710317