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Cloning, characterization and functional expression of an alkalitolerant type C feruloyl esterase from Fusarium oxysporum

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dc.contributor.author Moukouli, M en
dc.contributor.author Topakas, E en
dc.contributor.author Christakopoulos, P en
dc.date.accessioned 2014-03-01T01:28:02Z
dc.date.available 2014-03-01T01:28:02Z
dc.date.issued 2008 en
dc.identifier.issn 0175-7598 en
dc.identifier.uri http://hdl.handle.net/123456789/18677
dc.subject Alkalitolerant en
dc.subject Expression en
dc.subject Feruloyl esterase en
dc.subject Fusarium oxysporum en
dc.subject Gene cloning en
dc.subject Pichia pastoris en
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.other Alkalitolerant en
dc.subject.other Feruloyl esterase en
dc.subject.other Fusarium oxysporum en
dc.subject.other Pichia pastoris en
dc.subject.other Amino acids en
dc.subject.other Cloning en
dc.subject.other Enzyme activity en
dc.subject.other Hydrolysis en
dc.subject.other Molecular weight en
dc.subject.other Yeast en
dc.subject.other Gene expression en
dc.subject.other alcohol oxidase en
dc.subject.other alkyl group en
dc.subject.other benzene derivative en
dc.subject.other coumaric acid en
dc.subject.other ester derivative en
dc.subject.other esterase en
dc.subject.other ferulic acid en
dc.subject.other feruloyl esterase en
dc.subject.other fungal DNA en
dc.subject.other fungal enzyme en
dc.subject.other glycoside en
dc.subject.other mating hormone alpha factor en
dc.subject.other methyl group en
dc.subject.other nitro derivative en
dc.subject.other recombinant enzyme en
dc.subject.other serine proteinase en
dc.subject.other unclassified drug en
dc.subject.other xylan endo 1,3 beta xylosidase en
dc.subject.other clone en
dc.subject.other enzyme activity en
dc.subject.other fungus en
dc.subject.other gene expression en
dc.subject.other hydrolysis en
dc.subject.other tolerance en
dc.subject.other yeast en
dc.subject.other amino acid sequence en
dc.subject.other AOX1 gene en
dc.subject.other article en
dc.subject.other enzyme activity en
dc.subject.other enzyme analysis en
dc.subject.other enzyme specificity en
dc.subject.other enzyme stability en
dc.subject.other enzyme substrate en
dc.subject.other Fusarium oxysporum en
dc.subject.other genetic conservation en
dc.subject.other hydrolysis en
dc.subject.other molecular cloning en
dc.subject.other molecular weight en
dc.subject.other nonhuman en
dc.subject.other paper industry en
dc.subject.other pH en
dc.subject.other Pichia pastoris en
dc.subject.other promoter region en
dc.subject.other protein expression en
dc.subject.other protein motif en
dc.subject.other pulp mill en
dc.subject.other Saccharomyces cerevisiae en
dc.subject.other signal transduction en
dc.subject.other transcription regulation en
dc.subject.other Trichoderma en
dc.subject.other trichoderma longibrachiatum en
dc.subject.other wheat bran en
dc.subject.other Carboxylic Ester Hydrolases en
dc.subject.other Cloning, Molecular en
dc.subject.other Coumaric Acids en
dc.subject.other Fusarium en
dc.subject.other Gene Expression Regulation, Fungal en
dc.subject.other Hydrogen-Ion Concentration en
dc.subject.other Industrial Microbiology en
dc.subject.other Molecular Weight en
dc.subject.other Recombinant Proteins en
dc.subject.other Saccharomyces cerevisiae en
dc.subject.other Substrate Specificity en
dc.subject.other Fusarium oxysporum en
dc.subject.other Pichia pastoris en
dc.subject.other Saccharomyces cerevisiae en
dc.subject.other Trichoderma longibrachiatum en
dc.subject.other Triticum aestivum en
dc.title Cloning, characterization and functional expression of an alkalitolerant type C feruloyl esterase from Fusarium oxysporum en
heal.type journalArticle en
heal.identifier.primary 10.1007/s00253-008-1432-3 en
heal.identifier.secondary http://dx.doi.org/10.1007/s00253-008-1432-3 en
heal.language English en
heal.publicationDate 2008 en
heal.abstract A hypothetical protein FoFaeC-12213 of Fusarium oxysporum was found to have high amino acid sequence identity with known type C feruloyl esterases (FAEs) containing a 13-amino acid conserved region flanking the characteristic G-X-S-X-G motif of a serine esterase. The putative FAE from the genomic DNA was successfully cloned in frame with the Saccharomyces cerevisiae α-factor secretion signal under the transcriptional control of the alcohol oxidase (AOX1) promoter and integrated in Pichia pastoris X-33 to confirm that the enzyme exhibits FAE activity. The molecular weight (62 kDa) and p I (6.8) were in agreement with the theoretical calculated values indicating the correct processing of the secretion signal in P. pastoris. The recombinant FAE was purified to its homogeneity and subsequently characterized using a series of model substrates including methyl esters of hydroxycinnamates, alkyl ferulates and monoferuloylated 4-nitrophenyl glycosides. The substrate specificity profiling reveals that the enzyme is a type C FAE showing broad hydrolytic activity against the four methyl esters of hydroxycinnamic acids and strong preference for the hydrolysis of n-propyl ferulate. Ferulic acid (FA) was efficiently released from destarched wheat bran when the esterase was incubated together with xylanase from Trichoderma longibrachiatum (a maximum of 67% total FA released after 1-h incubation). The esterase showed broad pH stability making it an important candidate for alkaline applications such as pulp treatment in the paper industry. © 2008 Springer-Verlag. en
heal.publisher Springer-Verlag en
heal.journalName Applied Microbiology and Biotechnology en
dc.identifier.doi 10.1007/s00253-008-1432-3 en
dc.identifier.isi ISI:000255253200010 en
dc.identifier.volume 79 en
dc.identifier.issue 2 en
dc.identifier.spage 245 en
dc.identifier.epage 254 en


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