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Article: Penicillium brasilianum as an enzyme factory; the essential role of feruloyl esterases for the hydrolysis of the plant cell wall

TitlePenicillium brasilianum as an enzyme factory; the essential role of feruloyl esterases for the hydrolysis of the plant cell wall
Authors
KeywordsArabinoxylan degradation
Feruloyl esterase
Plant cell wall
Response surface methodology
Issue Date2007
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/jbiotec
Citation
Journal Of Biotechnology, 2007, v. 130 n. 3, p. 219-228 How to Cite?
AbstractThe production of arabinoxylan-degrading enzymes by the fungus Penicillium brasilianum, grown on different carbon and nitrogen sources as well as different environmental conditions was investigated. Highest feruloyl esterase (225 mU/ml) and α-l-arabinofuranosidase (211 mU/ml) activities were obtained when P. brasilianum was grown on sugar beet pulp, whereas maximum xylanase (17 U/ml) activity was found during growth on oat spelt xylan. Yeast extract was the preferable nitrogen source for the production of all the three enzymes. Further optimization of the production of the crude enzyme mixture was examined by experimental design using a d-optimal quadratic model. Investigation of the microbial regulation of enzyme production showed that the presence of free ferulic acid further stimulated the production and pointing to that the fungal regulatory mechanism involved a coordinated production and secretion of feruloyl esterase, xylanase and α-l-arabinofuranosidase. Since agroindustrial by-products are a potential source of phenolic acids, crude enzyme mixtures of P. brasilianum were tested for their hydrolysis abilities against eight complex or model substrates. While total release of phenolic acids and pentoses was not observed, the synergistic enhancement of hydrolysis in the presence of feruloyl esterase was clearly demonstrated. © 2007 Elsevier B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/181244
ISSN
2023 Impact Factor: 4.1
2023 SCImago Journal Rankings: 0.741
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorPanagiotou, Gen_US
dc.contributor.authorOlavarria, Ren_US
dc.contributor.authorOlsson, Len_US
dc.date.accessioned2013-02-21T02:03:27Z-
dc.date.available2013-02-21T02:03:27Z-
dc.date.issued2007en_US
dc.identifier.citationJournal Of Biotechnology, 2007, v. 130 n. 3, p. 219-228en_US
dc.identifier.issn0168-1656en_US
dc.identifier.urihttp://hdl.handle.net/10722/181244-
dc.description.abstractThe production of arabinoxylan-degrading enzymes by the fungus Penicillium brasilianum, grown on different carbon and nitrogen sources as well as different environmental conditions was investigated. Highest feruloyl esterase (225 mU/ml) and α-l-arabinofuranosidase (211 mU/ml) activities were obtained when P. brasilianum was grown on sugar beet pulp, whereas maximum xylanase (17 U/ml) activity was found during growth on oat spelt xylan. Yeast extract was the preferable nitrogen source for the production of all the three enzymes. Further optimization of the production of the crude enzyme mixture was examined by experimental design using a d-optimal quadratic model. Investigation of the microbial regulation of enzyme production showed that the presence of free ferulic acid further stimulated the production and pointing to that the fungal regulatory mechanism involved a coordinated production and secretion of feruloyl esterase, xylanase and α-l-arabinofuranosidase. Since agroindustrial by-products are a potential source of phenolic acids, crude enzyme mixtures of P. brasilianum were tested for their hydrolysis abilities against eight complex or model substrates. While total release of phenolic acids and pentoses was not observed, the synergistic enhancement of hydrolysis in the presence of feruloyl esterase was clearly demonstrated. © 2007 Elsevier B.V. All rights reserved.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/jbiotecen_US
dc.relation.ispartofJournal of Biotechnologyen_US
dc.subjectArabinoxylan degradation-
dc.subjectFeruloyl esterase-
dc.subjectPlant cell wall-
dc.subjectResponse surface methodology-
dc.subject.meshAnalysis Of Varianceen_US
dc.subject.meshCarbon - Metabolismen_US
dc.subject.meshCarboxylic Ester Hydrolases - Metabolismen_US
dc.subject.meshCell Wall - Drug Effects - Metabolismen_US
dc.subject.meshCoumaric Acids - Metabolism - Pharmacologyen_US
dc.subject.meshEnzyme Inductionen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshHydrolysis - Drug Effectsen_US
dc.subject.meshNitrogen - Metabolismen_US
dc.subject.meshPenicillium - Enzymologyen_US
dc.subject.meshPentoses - Metabolismen_US
dc.subject.meshPlants - Drug Effects - Metabolismen_US
dc.subject.meshTemperatureen_US
dc.subject.meshTime Factorsen_US
dc.titlePenicillium brasilianum as an enzyme factory; the essential role of feruloyl esterases for the hydrolysis of the plant cell wallen_US
dc.typeArticleen_US
dc.identifier.emailPanagiotou, G: gipa@hku.hken_US
dc.identifier.authorityPanagiotou, G=rp01725en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.jbiotec.2007.04.011en_US
dc.identifier.pmid17544537-
dc.identifier.scopuseid_2-s2.0-34250663590en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34250663590&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume130en_US
dc.identifier.issue3en_US
dc.identifier.spage219en_US
dc.identifier.epage228en_US
dc.identifier.isiWOS:000248109600003-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridPanagiotou, G=8566179700en_US
dc.identifier.scopusauthoridOlavarria, R=35080934200en_US
dc.identifier.scopusauthoridOlsson, L=7203077540en_US
dc.identifier.issnl0168-1656-

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