Purification and characterization of an inducible p-coumaric acid decarboxylase from Lactobacillus plantarum
- Author
- Jean-François Cavin, Lise Barthelmebs, Jean Guzzo, Jozef Van Beeumen (UGent) , Bart Samyn (UGent) , Jean-François Travers and Charles Diviès
- Organization
- 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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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-182132
- MLA
- Cavin, Jean-François, et al. “Purification and Characterization of an Inducible P-Coumaric Acid Decarboxylase from Lactobacillus Plantarum.” FEMS MICROBIOLOGY LETTERS, vol. 147, no. 2, 1997, pp. 291–95, doi:10.1111/j.1574-6968.1997.tb10256.x.
- 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. https://doi.org/10.1111/j.1574-6968.1997.tb10256.x
- Chicago author-date
- 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): 291–95. https://doi.org/10.1111/j.1574-6968.1997.tb10256.x.
- Chicago author-date (all authors)
- 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. doi:10.1111/j.1574-6968.1997.tb10256.x.
- 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.
- IEEE
- [1]J.-F. Cavin et al., “Purification and characterization of an inducible p-coumaric acid decarboxylase from Lactobacillus plantarum,” FEMS MICROBIOLOGY LETTERS, vol. 147, no. 2, pp. 291–295, 1997.
@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 (< 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-François and Barthelmebs, Lise and Guzzo, Jean and Van Beeumen, Jozef and Samyn, Bart and Travers, Jean-François and Diviès, Charles}},
issn = {{0378-1097}},
journal = {{FEMS MICROBIOLOGY LETTERS}},
keywords = {{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://doi.org/10.1111/j.1574-6968.1997.tb10256.x}},
volume = {{147}},
year = {{1997}},
}
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