This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Smit, B. A.
Right arrow Articles by Smit, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Smit, B. A.
Right arrow Articles by Smit, G.
Agricola
Right arrow Articles by Smit, B. A.
Right arrow Articles by Smit, G.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, January 2005, p. 303-311, Vol. 71, No. 1
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.1.303-311.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Identification, Cloning, and Characterization of a Lactococcus lactis Branched-Chain {alpha}-Keto Acid Decarboxylase Involved in Flavor Formation

Bart A. Smit,1 Johan E. T. van Hylckama Vlieg,1 Wim J. M. Engels,1* Laura Meijer,1 Jan T. M. Wouters,2 and Gerrit Smit1,2

Department of Flavor, Nutrition and Ingredients, NIZO food research, Ede,1 Department of Agrotechnology and Food Sciences, Wageningen University, Wageningen, The Netherlands2

Received 8 February 2004/ Accepted 29 August 2004

The biochemical pathway for formation of branched-chain aldehydes, which are important flavor compounds derived from proteins in fermented dairy products, consists of a protease, peptidases, a transaminase, and a branched-chain {alpha}-keto acid decarboxylase (KdcA). The activity of the latter enzyme has been found only in a limited number of Lactococcus lactis strains. By using a random mutagenesis approach, the gene encoding KdcA in L. lactis B1157 was identified. The gene for this enzyme is highly homologous to the gene annotated ipd, which encodes a putative indole pyruvate decarboxylase, in L. lactis IL1403. Strain IL1403 does not produce KdcA, which could be explained by a 270-nucleotide deletion at the 3' terminus of the ipd gene encoding a truncated nonfunctional decarboxylase. The kdcA gene was overexpressed in L. lactis for further characterization of the decarboxylase enzyme. Of all of the potential substrates tested, the highest activity was observed with branched-chain {alpha}-keto acids. Moreover, the enzyme activity was hardly affected by high salinity, and optimal activity was found at pH 6.3, indicating that the enzyme might be active under cheese ripening conditions.


* Corresponding author. Mailing address: NIZO food research, Department of Flavor, Nutrition and Ingredients, P.O. Box 20, 6710 BA Ede, The Netherlands. Phone: 31 318659532. Fax: 31 318650400. E-mail: Wim.Engels{at}nizo.nl.


Applied and Environmental Microbiology, January 2005, p. 303-311, Vol. 71, No. 1
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.1.303-311.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Bachmann, H., Kruijswijk, Z., Molenaar, D., Kleerebezem, M., van Hylckama Vlieg, J. E. T. (2009). A high-throughput cheese manufacturing model for effective cheese starter culture screening. J DAIRY SCI 92: 5868-5882 [Abstract] [Full Text]  
  • Atsumi, S., Li, Z., Liao, J. C. (2009). Acetolactate Synthase from Bacillus subtilis Serves as a 2-Ketoisovalerate Decarboxylase for Isobutanol Biosynthesis in Escherichia coli. Appl. Environ. Microbiol. 75: 6306-6311 [Abstract] [Full Text]  
  • Tachon, S., Michelon, D., Chambellon, E., Cantonnet, M., Mezange, C., Henno, L., Cachon, R., Yvon, M. (2009). Experimental conditions affect the site of tetrazolium violet reduction in the electron transport chain of Lactococcus lactis. Microbiology 155: 2941-2948 [Abstract] [Full Text]  
  • Chambellon, E., Rijnen, L., Lorquet, F., Gitton, C., van Hylckama Vlieg, J. E. T., Wouters, J. A., Yvon, M. (2009). The D-2-Hydroxyacid Dehydrogenase Incorrectly Annotated PanE Is the Sole Reduction System for Branched-Chain 2-Keto Acids in Lactococcus lactis. J. Bacteriol. 191: 873-881 [Abstract] [Full Text]  
  • Liu, M., Nauta, A., Francke, C., Siezen, R. J. (2008). Comparative Genomics of Enzymes in Flavor-Forming Pathways from Amino Acids in Lactic Acid Bacteria. Appl. Environ. Microbiol. 74: 4590-4600 [Full Text]  
  • Werther, T., Spinka, M., Tittmann, K., Schutz, A., Golbik, R., Mrestani-Klaus, C., Hubner, G., Konig, S. (2008). Amino Acids Allosterically Regulate the Thiamine Diphosphate-dependent {alpha}-Keto Acid Decarboxylase from Mycobacterium tuberculosis. J. Biol. Chem. 283: 5344-5354 [Abstract] [Full Text]  
  • Siezen, R. J., Starrenburg, M. J. C., Boekhorst, J., Renckens, B., Molenaar, D., van Hylckama Vlieg, J. E. T. (2008). Genome-Scale Genotype-Phenotype Matching of Two Lactococcus lactis Isolates from Plants Identifies Mechanisms of Adaptation to the Plant Niche. Appl. Environ. Microbiol. 74: 424-436 [Abstract] [Full Text]  
  • Whetstine, M. E. C., Drake, M. A., Broadbent, J. R., McMahon, D. (2006). Enhanced Nutty Flavor Formation in Cheddar Cheese Made with a Malty Lactococcus lactis Adjunct Culture.. J DAIRY SCI 89: 3277-3284 [Abstract] [Full Text]  
  • Tanous, C., Chambellon, E., Le Bars, D., Delespaul, G., Yvon, M. (2006). Glutamate Dehydrogenase Activity Can Be Transmitted Naturally to Lactococcus lactis Strains To Stimulate Amino Acid Conversion to Aroma Compounds. Appl. Environ. Microbiol. 72: 1402-1409 [Abstract] [Full Text]  
  • Siegert, P., McLeish, M. J., Baumann, M., Iding, H., Kneen, M. M., Kenyon, G. L., Pohl, M. (2005). Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida. Protein Eng Des Sel 18: 345-357 [Abstract] [Full Text]