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Purification, characterization and mass spectrometric sequencing of a thermophilic glucuronoyl esterase from Sporotrichum thermophile

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dc.contributor.author Vafiadi, C en
dc.contributor.author Topakas, E en
dc.contributor.author Biely, P en
dc.contributor.author Christakopoulos, P en
dc.date.accessioned 2014-03-01T01:31:44Z
dc.date.available 2014-03-01T01:31:44Z
dc.date.issued 2009 en
dc.identifier.issn 0378-1097 en
dc.identifier.uri https://dspace.lib.ntua.gr/xmlui/handle/123456789/19911
dc.subject Glucuronoyl esterase en
dc.subject Lignin-carbohydrate complex en
dc.subject Mass spectrometric sequencing en
dc.subject Purification en
dc.subject Sporotrichum thermophile en
dc.subject.classification Microbiology en
dc.subject.other esterase en
dc.subject.other glucuronoyl esterase 1 en
dc.subject.other pyranoside en
dc.subject.other unclassified drug en
dc.subject.other article en
dc.subject.other catalysis en
dc.subject.other enzyme activity en
dc.subject.other enzyme analysis en
dc.subject.other enzyme purification en
dc.subject.other enzyme stability en
dc.subject.other enzyme synthesis en
dc.subject.other fungus en
dc.subject.other gene sequence en
dc.subject.other mass spectrometry en
dc.subject.other mesophile en
dc.subject.other molecular weight en
dc.subject.other nonhuman en
dc.subject.other nucleotide sequence en
dc.subject.other pH en
dc.subject.other priority journal en
dc.subject.other sequence homology en
dc.subject.other sporotrichum thermophile en
dc.subject.other temperature en
dc.subject.other Amino Acid Sequence en
dc.subject.other Enzyme Stability en
dc.subject.other Fungal Proteins en
dc.subject.other Glucuronates en
dc.subject.other Glucuronidase en
dc.subject.other Hydrogen-Ion Concentration en
dc.subject.other Isoelectric Point en
dc.subject.other Lignin en
dc.subject.other Mass Spectrometry en
dc.subject.other Molecular Sequence Data en
dc.subject.other Molecular Weight en
dc.subject.other Sequence Homology, Amino Acid en
dc.subject.other Sporothrix en
dc.subject.other Substrate Specificity en
dc.subject.other Temperature en
dc.subject.other Xylans en
dc.subject.other Chaetomium globosum CBS 148.51 en
dc.subject.other Corynascus heterothallicus en
dc.subject.other Fungi en
dc.title Purification, characterization and mass spectrometric sequencing of a thermophilic glucuronoyl esterase from Sporotrichum thermophile en
heal.type journalArticle en
heal.identifier.primary 10.1111/j.1574-6968.2009.01631.x en
heal.identifier.secondary http://dx.doi.org/10.1111/j.1574-6968.2009.01631.x en
heal.language English en
heal.publicationDate 2009 en
heal.abstract The cellulolytic system of the thermophilic fungus Sporotrichum thermophile contains a recently discovered esterase that may hydrolyze the ester linkage between the 4-O-methyl-d-glucuronic acid of glucuronoxylan and lignin alcohols. The glucuronoyl esterase named StGE1 was purified to homogeneity with a molecular mass of Mr 58 kDa and pI 6.7. The enzyme activity was optimal at pH 6.0 and 60 °C. The esterase displayed a narrow pH range stability at pH 8.0 and retained 50% of its activity after 430 and 286 min at 50 and 55 °C, respectively. The enzyme was active on substrates containing glucuronic acid methyl ester, showing a lower catalytic efficiency on 4-nitrophenyl 2-O-(methyl-4-O-methyl-α-d-glucopyranosyluronate)-β-d- xylopyranoside than its mesophilic counterparts reported in the literature, which is typical of thermophilic enzymes. StGE1 was proved to be a modular enzyme containing a noncatalytic carbohydrate-binding module. LC-MS/MS analysis provided peptide mass and sequence information that facilitated the identification and classification of StGE1 as a family 15 glucuronoyl esterase that showed the highest homology with the hypothetical glucuronoyl esterase CHGG-10774 of Chaetomium globosum CBS 148.51. This work represents the first example of the purification and identification of a thermophilic glucuronoyl esterase from S. thermophile. © 2009 Federation of European Microbiological Societies. en
heal.publisher WILEY-BLACKWELL PUBLISHING, INC en
heal.journalName FEMS Microbiology Letters en
dc.identifier.doi 10.1111/j.1574-6968.2009.01631.x en
dc.identifier.isi ISI:000266979400005 en
dc.identifier.volume 296 en
dc.identifier.issue 2 en
dc.identifier.spage 178 en
dc.identifier.epage 184 en


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