Source:http://linkedlifedata.com/resource/pubmed/id/19050833
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2009-9-3
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pubmed:abstractText |
A novel endoxanthanase was produced and isolated from the culture of Microbacterium sp. XT11 growing on xanthan. Optimum pH and temperature for the enzyme activity were 6.0 and 35-40 degrees C, respectively. The endoxanthanase cleaves the backbone endo-beta-1,4-glucosidic linkage of the xanthan molecule, which is specific to the intact xanthan. However, the lyase-treated xanthan or carboxymethyl cellulose could not be cleaved by endoxanthanase.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1559-0291
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
159
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
24-32
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pubmed:meshHeading |
pubmed-meshheading:19050833-Binding Sites,
pubmed-meshheading:19050833-Endo-1,3(4)-beta-Glucanase,
pubmed-meshheading:19050833-Enzyme Activation,
pubmed-meshheading:19050833-Enzyme Stability,
pubmed-meshheading:19050833-Gram-Positive Bacteria,
pubmed-meshheading:19050833-Hydrolysis,
pubmed-meshheading:19050833-Polysaccharides, Bacterial,
pubmed-meshheading:19050833-Protein Binding
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pubmed:year |
2009
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pubmed:articleTitle |
Endoxanthanase, a novel beta-D-glucanase hydrolyzing backbone linkage of intact xanthan from newly isolated Microbacterium sp. XT11.
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pubmed:affiliation |
Department of Bio & Food Engineering, Dalian College of Light Industry, Dalian, People's Republic of China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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