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Purification and characterization of an inducible p-coumaric acid decarboxylase from Lactobacillus plantarum

(1997) FEMS MICROBIOLOGY LETTERS. 147(2). p.291-295
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Abstract
Lactobacillus plantarum cells displayed substrate-inducible decarboxylase activities on p-coumaric and ferulic acids of 0.6 and 0.01 mu mol min(-1) mg(-1), respectively. Activity in uninduced cells or corresponding cell extracts was undetectable (< 10(-4) mu mol min(-1) mg(-1)). Specificity of induction indicates that at least two phenolic acid decarboxylases are produced in this bacterium. SDS-PAGE of partially purified protein extract from p-coumaric acid-induced cells showed one band of 23.5 kDa that was absent in the extract from uninduced cells, The native molecular mass of 93 kDa indicates that the enzyme is a homotetramer. The 1276-fold purified enzyme had a K-m of 1.4 mM, a V-m of about 766 mu mol min(-1) mg(-1), and a K-cat of 10(3) s(-1) for p-coumaric and caffeic acids, but did not display any detectable activity on ferulic acid. Maximum activity was at 30 degrees C, at pH 5.5-6, Cofactors or metal ions were not required for activity.
Keywords
decarboxylase, Lactobacillus plantarum, p-coumaric acid, ferulic acid, caffeic acid, VOLATILE PHENOLS, BACILLUS-PUMILUS, BACTERIA, WINES

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Chicago
Cavin, Jean-François, Lise Barthelmebs, Jean Guzzo, Jozef Van Beeumen, Bart Samyn, Jean-François Travers, and Charles Diviès. 1997. “Purification and Characterization of an Inducible P-coumaric Acid Decarboxylase from Lactobacillus Plantarum.” Fems Microbiology Letters 147 (2): 291–295.
APA
Cavin, J.-F., Barthelmebs, L., Guzzo, J., Van Beeumen, J., Samyn, B., Travers, J.-F., & Diviès, C. (1997). Purification and characterization of an inducible p-coumaric acid decarboxylase from Lactobacillus plantarum. FEMS MICROBIOLOGY LETTERS, 147(2), 291–295.
Vancouver
1.
Cavin J-F, Barthelmebs L, Guzzo J, Van Beeumen J, Samyn B, Travers J-F, et al. Purification and characterization of an inducible p-coumaric acid decarboxylase from Lactobacillus plantarum. FEMS MICROBIOLOGY LETTERS. 1997;147(2):291–5.
MLA
Cavin, Jean-François, Lise Barthelmebs, Jean Guzzo, et al. “Purification and Characterization of an Inducible P-coumaric Acid Decarboxylase from Lactobacillus Plantarum.” FEMS MICROBIOLOGY LETTERS 147.2 (1997): 291–295. Print.
@article{182132,
  abstract     = {Lactobacillus plantarum cells displayed substrate-inducible decarboxylase activities on p-coumaric and ferulic acids of 0.6 and 0.01 mu mol min(-1) mg(-1), respectively. Activity in uninduced cells or corresponding cell extracts was undetectable ({\textlangle} 10(-4) mu mol min(-1) mg(-1)). Specificity of induction indicates that at least two phenolic acid decarboxylases are produced in this bacterium. SDS-PAGE of partially purified protein extract from p-coumaric acid-induced cells showed one band of 23.5 kDa that was absent in the extract from uninduced cells, The native molecular mass of 93 kDa indicates that the enzyme is a homotetramer. The 1276-fold purified enzyme had a K-m of 1.4 mM, a V-m of about 766 mu mol min(-1) mg(-1), and a K-cat of 10(3) s(-1) for p-coumaric and caffeic acids, but did not display any detectable activity on ferulic acid. Maximum activity was at 30 degrees C, at pH 5.5-6, Cofactors or metal ions were not required for activity.},
  author       = {Cavin, Jean-Fran\c{c}ois and Barthelmebs, Lise and Guzzo, Jean and Van Beeumen, Jozef and Samyn, Bart and Travers, Jean-Fran\c{c}ois and Divi{\`e}s, Charles},
  issn         = {0378-1097},
  journal      = {FEMS MICROBIOLOGY LETTERS},
  keyword      = {decarboxylase,Lactobacillus plantarum,p-coumaric acid,ferulic acid,caffeic acid,VOLATILE PHENOLS,BACILLUS-PUMILUS,BACTERIA,WINES},
  language     = {eng},
  number       = {2},
  pages        = {291--295},
  title        = {Purification and characterization of an inducible p-coumaric acid decarboxylase from Lactobacillus plantarum},
  url          = {http://dx.doi.org/10.1111/j.1574-6968.1997.tb10256.x},
  volume       = {147},
  year         = {1997},
}

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