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Applied and Environmental Microbiology, October 1998, p. 3765-3768, Vol. 64, No. 10
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Xanthan Lyase of Bacillus sp. Strain GL1 Liberates Pyruvylated Mannose from Xanthan Side Chains

Wataru Hashimoto,1,* Hikaru Miki,1 Noriaki Tsuchiya,2 Hirokazu Nankai,1 and Kousaku Murata1

Research Institute for Food Science, Kyoto University, Uji, Kyoto 611-0011,1 and Food & Food Additives Research Laboratories, Dainippon Pharmaceutical Co., Ltd., Suita, Osaka 564-0053,2 Japan

Received 29 December 1997/Accepted 31 July 1998

When the bacterium Bacillus sp. strain GL1 was grown in a medium containing xanthan as the carbon source, the viscosity of the medium decreased in association with growth, showing that the bacterium had xanthan-depolymerizing enzymes. One of the xanthan-depolymerizing enzymes (xanthan lyase) was present in the medium and was found to be induced by xanthan. The xanthan lyase purified from the culture fluid was a monomer with a molecular mass of 75 kDa, and was most active at pH 5.5 and 50°C. The enzyme was highly specific for xanthan and produced pyruvylated mannose. The result indicates that the enzyme cleaved the linkage between the terminal pyruvylated mannosyl and glucuronyl residues in the side chain of xanthan.

* Corresponding author. Mailing address: Research Institute for Food Science, Kyoto University, Uji 611-0011, Japan. Phone: 81-774-38-3768. Fax: 81-774-38-3767. E-mail: hasimoto{at}food2.food.kyoto-u.ac.jp.

Applied and Environmental Microbiology, October 1998, p. 3765-3768, Vol. 64, No. 10
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Hashimoto, W., Nankai, H., Mikami, B., Murata, K. (2003). Crystal Structure of Bacillus sp. GL1 Xanthan Lyase, Which Acts on the Side Chains of Xanthan. J. Biol. Chem. 278: 7663-7673 [Abstract] [Full Text]  
  • Nankai, H., Hashimoto, W., Murata, K. (2002). Molecular Identification of Family 38 {alpha}-Mannosidase of Bacillus sp. Strain GL1, Responsible for Complete Depolymerization of Xanthan. Appl. Environ. Microbiol. 68: 2731-2736 [Abstract] [Full Text]  
  • Da Costa, A., Michaud, P., Petit, E., Heyraud, A., Colin-Morel, P., Courtois, B., Courtois, J. (2001). Purification and Properties of a Glucuronan Lyase from Sinorhizobium meliloti M5N1CS (NCIMB 40472). Appl. Environ. Microbiol. 67: 5197-5203 [Abstract] [Full Text]  
  • Hashimoto, W., Miki, H., Tsuchiya, N., Nankai, H., Murata, K. (2001). Polysaccharide Lyase: Molecular Cloning, Sequencing, and Overexpression of the Xanthan Lyase Gene of Bacillus sp. Strain GL1. Appl. Environ. Microbiol. 67: 713-720 [Abstract] [Full Text]  
  • Ruijssenaars, H. J., Hartmans, S., Verdoes, J. C. (2000). A Novel Gene Encoding Xanthan Lyase of Paenibacillus alginolyticus Strain XL-1. Appl. Environ. Microbiol. 66: 3945-3950 [Abstract] [Full Text]  
  • Ruijssenaars, H. J., de Bont, J. A. M., Hartmans, S. (1999). A Pyruvated Mannose-Specific Xanthan Lyase Involved in Xanthan Degradation by Paenibacillus alginolyticus XL-1. Appl. Environ. Microbiol. 65: 2446-2452 [Abstract] [Full Text]  
  • Nankai, H., Hashimoto, W., Miki, H., Kawai, S., Murata, K. (1999). Microbial System for Polysaccharide Depolymerization: Enzymatic Route for Xanthan Depolymerization by Bacillus sp. Strain GL1. Appl. Environ. Microbiol. 65: 2520-2526 [Abstract] [Full Text]  


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