Characterization of thep-Coumaric Acid Decarboxylase from Lactobacillus plantarum CECT 748T

2008 ◽  
Vol 56 (9) ◽  
pp. 3068-3072 ◽  
Author(s):  
Héctor Rodríguez ◽  
José María Landete ◽  
José Antonio Curiel ◽  
Blanca de las Rivas ◽  
José Miguel Mancheño ◽  
...  
2006 ◽  
Vol 147 (2) ◽  
pp. 291-295 ◽  
Author(s):  
Jean-François Cavin ◽  
Lise Barthelmebs ◽  
Jean Guzzo ◽  
Jozef Beeumen ◽  
Bart Samyn ◽  
...  

2000 ◽  
Vol 66 (8) ◽  
pp. 3368-3375 ◽  
Author(s):  
Lise Barthelmebs ◽  
Charles Divies ◽  
Jean-François Cavin

ABSTRACT Lactobacillus plantarum NC8 contains a pdcgene coding for p-coumaric acid decarboxylase activity (PDC). A food grade mutant, designated LPD1, in which the chromosomalpdc gene was replaced with the deleted pdc gene copy, was obtained by a two-step homologous recombination process using an unstable replicative vector. The LPD1 mutant strain remained able to weakly metabolize p-coumaric and ferulic acids into vinyl derivatives or into substituted phenyl propionic acids. We have shown that L. plantarum has a second acid phenol decarboxylase enzyme, better induced with ferulic acid than withp-coumaric acid, which also displays inducible acid phenol reductase activity that is mostly active when glucose is added. Those two enzymatic activities are in competition for p-coumaric and ferulic acid degradation, and the ratio of the corresponding derivatives depends on induction conditions. Moreover, PDC appeared to decarboxylate ferulic acid in vitro with a specific activity of about 10 nmol · min−1 · mg−1 in the presence of ammonium sulfate. Finally, PDC activity was shown to confer a selective advantage on LPNC8 grown in acidic media supplemented withp-coumaric acid, compared to the LPD1 mutant devoid of PDC activity.


Gene ◽  
1998 ◽  
Vol 215 (2) ◽  
pp. 371-379 ◽  
Author(s):  
Makiko Kakikawa ◽  
Nobukatsu Watanabe ◽  
Tatsuya Funawatashi ◽  
Masaya Oki ◽  
Hiroo Yasukawa ◽  
...  

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