Literature DB >> 3921951

[Enzymatic synthesis of 3,4-dihydroxyphenyl-L-alanine by free and immobilized Citrobacter freundii cells].

K I Voĭvodov, I V Tysiachnaia, L S Gubnitskiĭ, V I Iakovleva, I V Berezin.   

Abstract

The Citrobacter freundii 62 cells immobilized in PAAG and possessing the tyrosine-phenol-lyase (TPL) activity catalyse the synthesis of 3,4-dihydroxyphenyl-L-alanine (DOPA) from pyrocatechol and ammonium pyruvate. The synthesis of DOPA was studied using both free and immobilized bacterial cells. When the concentration of pyrocatechol is over 0.1 M the TPL activity of the cells is inhibited. The concentration of pyrocatechol can be increased up to 0.3 M by using an equimolar mixture of pyrocatechol and boric acid. The addition of ascorbic acid as an antioxidant results in a lower TPL activity of both free and immobilized bacterial cells.

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Year:  1985        PMID: 3921951

Source DB:  PubMed          Journal:  Prikl Biokhim Mikrobiol        ISSN: 0555-1099


  1 in total

1.  Production of L-dihydroxyphenylalanine in Escherichia coli with the tyrosine phenol-lyase gene cloned from Erwinia herbicola.

Authors:  F Foor; N Morin; K A Bostian
Journal:  Appl Environ Microbiol       Date:  1993-09       Impact factor: 4.792

  1 in total

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