Production and partial characterisation of feruloyl esterase by Sporotrichum thermophile in solid-state fermentation

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dc.contributor.author Topakas, E en
dc.contributor.author Kalogeris, E en
dc.contributor.author Kekos, D en
dc.contributor.author Macris, BJ en
dc.contributor.author Christakopoulos, P en
dc.date.accessioned 2014-03-01T01:19:26Z
dc.date.available 2014-03-01T01:19:26Z
dc.date.issued 2003 en
dc.identifier.issn 0032-9592 en
dc.identifier.uri http://hdl.handle.net/123456789/15499
dc.subject Feruloyl esterases en
dc.subject Solid state culture en
dc.subject Sporotrichum thermophile en
dc.subject.classification Biochemistry & Molecular Biology en
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.classification Engineering, Chemical en
dc.subject.other Corynascus heterothallicus en
dc.subject.other Fungi en
dc.subject.other Sporothrix en
dc.subject.other Sporotrichum en
dc.subject.other Triticum aestivum en
dc.title Production and partial characterisation of feruloyl esterase by Sporotrichum thermophile in solid-state fermentation en
heal.type journalArticle en
heal.identifier.primary 10.1016/S0032-9592(03)00044-X en
heal.identifier.secondary http://dx.doi.org/10.1016/S0032-9592(03)00044-X en
heal.language English en
heal.publicationDate 2003 en
heal.abstract A number of factors affecting production of feruloyl esterase an enzyme that hydrolyse ester linkages of ferulic acid (FA) in plant cell walls, by the thermophylic fungus Sporotrichum thermophile under solid state fermentation (SSF) were investigated. Initial moisture content and type of carbon source were consecutively optimised. SSF in a laboratory horizontal bioreactor using the optimised medium allowed the production of 156 mU g(-1) of carbon source, which compared favourably with those reported for the other micro-organisms. Optimal esterase activity was observed at pH 8 and 60 degreesC. The activity of the esterase was measured on an insoluble feruloylated hemicellulose substrate (de-starched wheat bran (DSWB)). De-esterifcation of wheat straw yielded loss of feruloyl esterase production even though the supplementation of free FA comparable to the alkali-extractable levels of FA found in wheat straw. Chromogenic (fluorogenic) 4-methylumbelliferyl ferulate was used to characterise the multienzyme component, after separation by isoelectric focusing and native PAGE electrophoresis. The zymograms indicated one major esterase activity exhibiting pI and molecular mass values 5 and 27 kDa, respectively. (C) 2003 Elsevier Science Ltd. All rights reserved. en
heal.publisher ELSEVIER SCI LTD en
heal.journalName Process Biochemistry en
dc.identifier.doi 10.1016/S0032-9592(03)00044-X en
dc.identifier.isi ISI:000184064300004 en
dc.identifier.volume 38 en
dc.identifier.issue 11 en
dc.identifier.spage 1539 en
dc.identifier.epage 1543 en

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