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Applied and Environmental Microbiology, May 2007, p. 3034-3039, Vol. 73, No. 9
0099-2240/07/$08.00+0     doi:10.1128/AEM.02290-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Role of Cystathionine ß-Lyase in Catabolism of Amino Acids to Sulfur Volatiles by Genetic Variants of Lactobacillus helveticus CNRZ 32{triangledown}

Won-Jae Lee,1 Dattatreya S. Banavara,2 Joanne E. Hughes,3 Jason K. Christiansen,4 James L. Steele,5 Jeffery R. Broadbent,4 and Scott A. Rankin5*

Division of Animal Science and Technology, Gyeongsang National University, Jinju 660-701, South Korea,1 Mead Johnson Nutritionals, Evansville, Indiana 47721,2 Department of Biology,3 Department of Nutrition and Food Science,4 Utah State University, Logan, Utah 84322; and Department of Food Science, University of Wisconsin—Madison, Madison, Wisconsin 537065

Received 28 September 2006/ Accepted 26 February 2007

Catabolism of sulfur-containing amino acids plays an important role in the development of cheese flavor. During ripening, cystathionine ß-lyase (CBL) is believed to contribute to the formation of volatile sulfur compounds (VSCs) such as methanethiol and dimethyl disulfide. However, the role of CBL in the generation of VSCs from the catabolism of specific sulfur-containing amino acids is not well characterized. The objective of this study was to investigate the role of CBL in VSC formation by Lactobacillus helveticus CNRZ 32 using genetic variants of L. helveticus CNRZ 32 including the CBL-null mutant, complementation of the CBL-null mutant, and the CBL overexpression mutant. The formation of VSCs from methionine, cystathionine, and cysteine was determined in a model system using gas chromatography-mass spectrometry with solid-phase microextraction. With methionine as a substrate, CBL overexpression resulted in higher VSC production than that of wild-type L. helveticus CNRZ 32 or the CBL-null mutant. However, there were no differences in VSC production between the wild type and the CBL-null mutant. With cystathionine, methanethiol production was detected from the CBL overexpression variant and complementation of the CBL-null mutant, implying that CBL may be involved in the conversion of cystathionine to methanethiol. With cysteine, no differences in VSC formation were observed between the wild type and genetic variants, indicating that CBL does not contribute to the conversion of cysteine.

* Corresponding author. Mailing address: Department of Food Science, University of Wisconsin—Madison, 1605 Linden Drive, Madison, WI 53706-1565. Phone: (608) 263-2008. Fax: (608) 262-6872. E-mail: sarankin{at}wisc.edu

{triangledown} Published ahead of print on 2 March 2007.

Applied and Environmental Microbiology, May 2007, p. 3034-3039, Vol. 73, No. 9
0099-2240/07/$08.00+0     doi:10.1128/AEM.02290-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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  • Lo, R., Turner, M. S., Barry, D. G., Sreekumar, R., Walsh, T. P., Giffard, P. M. (2009). Cystathionine {gamma}-Lyase Is a Component of Cystine-Mediated Oxidative Defense in Lactobacillus reuteri BR11. J. Bacteriol. 191: 1827-1837 [Abstract] [Full Text]  
  • Irmler, S., Raboud, S., Beisert, B., Rauhut, D., Berthoud, H. (2008). Cloning and Characterization of Two Lactobacillus casei Genes Encoding a Cystathionine Lyase. Appl. Environ. Microbiol. 74: 99-106 [Abstract] [Full Text]  


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