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rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
8
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|
pubmed:dateCreated |
1991-12-6
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|
pubmed:abstractText |
We have engineered recombinant glucose isomerase (GI) from Actinoplanes missouriensis by site-directed mutagenesis to enhance its thermal stability in both the soluble and immobilized forms. Substitution of arginine for lysine at position 253, which lies at the dimer/dimer interface of the GI tetramer, produced the largest stabilization under model industrial conditions. We discuss our results in terms of a model in which chemical glycation of lysines by sugars in the industrial corn syrup substrate represents a major pathway of destabilization.
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pubmed:language |
eng
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pubmed:journal |
|
|
pubmed:citationSubset |
B
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pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
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|
pubmed:issn |
0733-222X
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:volume |
9
|
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pubmed:owner |
NLM
|
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pubmed:authorsComplete |
Y
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pubmed:pagination |
738-42
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:1367634-Aldose-Ketose Isomerases,
pubmed-meshheading:1367634-Carbohydrate Epimerases,
pubmed-meshheading:1367634-Cloning, Molecular,
pubmed-meshheading:1367634-Enzymes, Immobilized,
pubmed-meshheading:1367634-Escherichia coli,
pubmed-meshheading:1367634-Gram-Positive Bacteria,
pubmed-meshheading:1367634-Hydrogen-Ion Concentration,
pubmed-meshheading:1367634-Models, Molecular,
pubmed-meshheading:1367634-Mutagenesis,
pubmed-meshheading:1367634-Protein Engineering,
pubmed-meshheading:1367634-Solutions,
pubmed-meshheading:1367634-Thermodynamics
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|
pubmed:year |
1991
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|
pubmed:articleTitle |
Enhancing the thermostability of glucose isomerase by protein engineering.
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pubmed:affiliation |
Gist-brocades, Research & Development, Delft, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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