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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2011-1-3
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pubmed:abstractText |
Measurements of esterase activity by enzyme-coupled assays on monoacetates of 4-nitrophenyl ?-D-xylopyranoside and 4-nitrophenyl ?-L-arabinofuranoside showed that acetylxylan esterases of families 1, 4 and 5 produced by Trichoderma reesei and Penicillium purpurogenum have a strong preference for deacetylation of position 2 in xylopyranosides. The acetylxylan esterases exhibit only weak activity on acetylated arabinofuranosides, with 2-acetate as the best substrate. Acetyl esterases of family 16 produced by the same two fungi deacetylate in xylopyranosides preferentially positions 3 and 4. Their specific activity on arabinofuranosides is also much lower than on xylopyranosides, however, substantially greater than that in the case of typical acetylxylan esterases.
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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 |
Jan
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pubmed:issn |
1873-4863
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pubmed:author |
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pubmed:copyrightInfo |
© 2010 Elsevier B.V. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
10
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pubmed:volume |
151
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
137-42
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pubmed:meshHeading |
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pubmed:year |
2011
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pubmed:articleTitle |
Action of xylan deacetylating enzymes on monoacetyl derivatives of 4-nitrophenyl glycosides of ?-D-xylopyranose and ?-L-arabinofuranose.
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pubmed:affiliation |
Institute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, SK-84538 Bratislava, Slovakia. chempbsa@savba.sk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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