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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1999-9-8
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pubmed:abstractText |
The xanthan-degrading bacterium Paenibacillus alginolyticus XL-1, isolated from soil, degrades approximately 28% of the xanthan molecule and appears to leave the backbone intact. Several xanthan-degrading enzymes were excreted during growth on xanthan, including xanthan lyase. Xanthan lyase production was induced by xanthan and inhibited by glucose and low-molecular-weight enzymatic degradation products from xanthan. A xanthan lyase with a molecular mass of 85 kDa and a pI of 7.9 was purified and characterized. The enzyme is specific for pyruvated mannosyl side chain residues and optimally active at pH 6.0 and 55 degrees C.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0099-2240
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
65
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2446-52
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10347025-Bacillus,
pubmed-meshheading:10347025-Biodegradation, Environmental,
pubmed-meshheading:10347025-Carbohydrate Sequence,
pubmed-meshheading:10347025-Carbon-Oxygen Lyases,
pubmed-meshheading:10347025-Hydrogen-Ion Concentration,
pubmed-meshheading:10347025-Mannose,
pubmed-meshheading:10347025-Molecular Sequence Data,
pubmed-meshheading:10347025-Polysaccharides, Bacterial,
pubmed-meshheading:10347025-Pyruvates,
pubmed-meshheading:10347025-Substrate Specificity,
pubmed-meshheading:10347025-Temperature
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pubmed:year |
1999
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pubmed:articleTitle |
A pyruvated mannose-specific xanthan lyase involved in xanthan degradation by Paenibacillus alginolyticus XL-1.
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pubmed:affiliation |
Division of Industrial Microbiology, Department of Food Technology and Nutritional Sciences, Wageningen University, 6700 EV Wageningen, The Netherlands. Harald.Ruijssenaars@imb.ftns.wau.nl
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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