Xanthan lyase of Bacillus sp. strain GL1 liberates pyruvylated mannose from xanthan side chains.
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Hashimoto W, Miki H, Tsuchiya N, Nankai H, Murata K
Xanthan lyase of Bacillus sp. strain GL1 liberates pyruvylated mannose from xanthan side chains.
Appl Environ Microbiol. 1998 Oct;64(10):3765-8.
- PubMed ID
- 9758797 [ View in PubMed]
- Abstract
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 degrees 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.