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- Publisher Website: 10.1016/j.jbiotec.2007.04.011
- Scopus: eid_2-s2.0-34250663590
- PMID: 17544537
- WOS: WOS:000248109600003
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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
Title | Penicillium brasilianum as an enzyme factory; the essential role of feruloyl esterases for the hydrolysis of the plant cell wall |
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Authors | |
Keywords | Arabinoxylan degradation Feruloyl esterase Plant cell wall Response surface methodology |
Issue Date | 2007 |
Publisher | Elsevier 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? |
Abstract | The 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 Identifier | http://hdl.handle.net/10722/181244 |
ISSN | 2023 Impact Factor: 4.1 2023 SCImago Journal Rankings: 0.741 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
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dc.contributor.author | Panagiotou, G | en_US |
dc.contributor.author | Olavarria, R | en_US |
dc.contributor.author | Olsson, L | en_US |
dc.date.accessioned | 2013-02-21T02:03:27Z | - |
dc.date.available | 2013-02-21T02:03:27Z | - |
dc.date.issued | 2007 | en_US |
dc.identifier.citation | Journal Of Biotechnology, 2007, v. 130 n. 3, p. 219-228 | en_US |
dc.identifier.issn | 0168-1656 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/181244 | - |
dc.description.abstract | The 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.language | eng | en_US |
dc.publisher | Elsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/jbiotec | en_US |
dc.relation.ispartof | Journal of Biotechnology | en_US |
dc.subject | Arabinoxylan degradation | - |
dc.subject | Feruloyl esterase | - |
dc.subject | Plant cell wall | - |
dc.subject | Response surface methodology | - |
dc.subject.mesh | Analysis Of Variance | en_US |
dc.subject.mesh | Carbon - Metabolism | en_US |
dc.subject.mesh | Carboxylic Ester Hydrolases - Metabolism | en_US |
dc.subject.mesh | Cell Wall - Drug Effects - Metabolism | en_US |
dc.subject.mesh | Coumaric Acids - Metabolism - Pharmacology | en_US |
dc.subject.mesh | Enzyme Induction | en_US |
dc.subject.mesh | Hydrogen-Ion Concentration | en_US |
dc.subject.mesh | Hydrolysis - Drug Effects | en_US |
dc.subject.mesh | Nitrogen - Metabolism | en_US |
dc.subject.mesh | Penicillium - Enzymology | en_US |
dc.subject.mesh | Pentoses - Metabolism | en_US |
dc.subject.mesh | Plants - Drug Effects - Metabolism | en_US |
dc.subject.mesh | Temperature | en_US |
dc.subject.mesh | Time Factors | en_US |
dc.title | Penicillium brasilianum as an enzyme factory; the essential role of feruloyl esterases for the hydrolysis of the plant cell wall | en_US |
dc.type | Article | en_US |
dc.identifier.email | Panagiotou, G: gipa@hku.hk | en_US |
dc.identifier.authority | Panagiotou, G=rp01725 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1016/j.jbiotec.2007.04.011 | en_US |
dc.identifier.pmid | 17544537 | - |
dc.identifier.scopus | eid_2-s2.0-34250663590 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-34250663590&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 130 | en_US |
dc.identifier.issue | 3 | en_US |
dc.identifier.spage | 219 | en_US |
dc.identifier.epage | 228 | en_US |
dc.identifier.isi | WOS:000248109600003 | - |
dc.publisher.place | Netherlands | en_US |
dc.identifier.scopusauthorid | Panagiotou, G=8566179700 | en_US |
dc.identifier.scopusauthorid | Olavarria, R=35080934200 | en_US |
dc.identifier.scopusauthorid | Olsson, L=7203077540 | en_US |
dc.identifier.issnl | 0168-1656 | - |