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Knockout of the p-coumarate decarboxylase gene from Lactobacillus plantarum reveals the existence of two other inducible enzymatic activities involved in phenolic acid metabolism.

ABSTRACT: Lactobacillus plantarum NC8 contains a pdc gene coding for p-coumaric acid decarboxylase activity (PDC). A food grade mutant, designated LPD1, in which the chromosomal pdc 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 with p-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 with p-coumaric acid, compared to the LPD1 mutant devoid of PDC activity.

SUBMITTER: Barthelmebs L

PROVIDER: S-EPMC92157 | biostudies-literature | 2000 Aug

REPOSITORIES: biostudies-literature

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Knockout of the p-coumarate decarboxylase gene from Lactobacillus plantarum reveals the existence of two other inducible enzymatic activities involved in phenolic acid metabolism.

Barthelmebs L L Divies C C Cavin J F JF

Applied and environmental microbiology 20000801 8

Lactobacillus plantarum NC8 contains a pdc gene coding for p-coumaric acid decarboxylase activity (PDC). A food grade mutant, designated LPD1, in which the chromosomal pdc 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. plan ...[more]

PMID: 10919793

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Project description:Seaweeds are potentially excellent sources of bioactive metabolites that could represent useful leads in the development of new functional ingredients in pharmaceutical and cosmetic industries. In the last decade, new marine bioprocess technologies have allowed the isolation of substances with biological properties. The brown alga Sargassum muticum (Yendo) Fensholt (Ochrophyta) was enzymatically hydrolyzed to prepare water-soluble extracts by using six different commercially available carbohydrate-degrading enzymes and two proteases. Evaluation of 2,2-diphenyl-1-picrylhydrazyl (DPPH) and ferric reducing antioxidant power (FRAP) antioxidant, tyrosinase, elastase, and biofilm inhibition, antibacterial and antiviral activities as well as evaluation of cytotoxicity were realized for each extract. Total phenolic content was measured for extract characterization, and solid-phase extraction was useful to purify the enzymatic extract. Soluble total phenolic content of S. muticum Viscozyme extract was highest with 6.4% of dry weight. Enzymatic Celluclast and Viscozyme extracts had the lowest value of DPPH IC50 indicating a strong antiradical activity, 0.6 mg mL-1, in comparison with other enzymes. The ferric reducing antioxidant power ranged between 48.7 ?M Fe2+ Eq, digested with Viscozyme, and 60.8 ?M Fe2+ Eq, digested with Amyloglucosidase. Tyrosinase inhibition activity of S. muticum Neutrase extract was 41.3% higher compared to other enzymes. Elastase inhibition activity of S. muticum Shearzyme extract had highest activity (32.8%). All enzymatic extracts showed no cytotoxic effect towards the kidney Vero cells. Meanwhile, only S. muticum Neutrase and Alcalase extracts exhibited potential antiviral activity. In addition, S. muticum Viscozyme and Shearzyme extracts showed promising activity in suppressing the biofilm formation against Pseudomonas aeruginosa and Escherichia coli, respectively. Purification of S. muticum Viscozyme extracts by solid-phase extraction managed to concentrate the phenolic content and improve the bioactivity. These results indicate the promising potential of enzyme-assisted followed by solid-phase extraction in recovering phenolic content and in improving its bioactivity.

Dataset Information

Knockout of the p-coumarate decarboxylase gene from Lactobacillus plantarum reveals the existence of two other inducible enzymatic activities involved in phenolic acid metabolism.

Publications

Knockout of the p-coumarate decarboxylase gene from Lactobacillus plantarum reveals the existence of two other inducible enzymatic activities involved in phenolic acid metabolism.

Similar Datasets

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