Screening of white-rot fungi manganese peroxidases: a comparison between the specific activities of the enzyme from different native producers.
Identifieur interne : 000391 ( Main/Curation ); précédent : 000390; suivant : 000392Screening of white-rot fungi manganese peroxidases: a comparison between the specific activities of the enzyme from different native producers.
Auteurs : Juho J Rvinen [Finlande] ; Sanna Taskila ; Ritva Isom Ki ; Heikki OjamoSource :
- AMB Express [ 2191-0855 ] ; 2012.
Abstract
In this study manganese peroxidase (MnP) enzymes from selected white-rot fungi were isolated and compared for potential future recombinant production. White-rot fungi were cultivated in small-scale in liquid media and a simplified process was established for the purification of extracellular enzymes.Five lignin degrading organisms were selected (Bjerkandera sp., Phanerochaete (P.) chrysosporium, Physisporinus (P.) rivulosus, Phlebia (P.) radiata and Phlebia sp. Nf b19) and studied for MnP production in small-scale. Extracellular MnP activity was followed and cultivations were harvested at proximity of the peak activity. The production of MnPs varied in different organisms but was clearly regulated by inducing liquid media components (Mn2+, veratryl alcohol and malonate). In total 8 different MnP isoforms were purified.Results of this study reinforce the conception that MnPs from distinct organisms differ substantially in their properties. Production of the extracellular enzyme in general did not reach a substantial level. This further suggests that these native producers are not suitable for industrial scale production of the enzyme. The highest specific activities were observed with MnPs from P. chrysosporium (200 U mg-1), Phlebia sp. Nf b19 (55 U mg-1) and P. rivulosus (89 U mg-1) and these MnPs are considered as the most potential candidates for further studies. The molecular weight of the purified MnPs was estimated to be between 45-50 kDa.
DOI: 10.1186/2191-0855-2-62
PubMed: 23190610
PubMed Central: PMC3549895
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Screening of white-rot fungi manganese peroxidases: a comparison between the specific activities of the enzyme from different native producers.</title><author><name sortKey="J Rvinen, Juho" sort="J Rvinen, Juho" uniqKey="J Rvinen J" first="Juho" last="J Rvinen">Juho J Rvinen</name><affiliation wicri:level="1"><nlm:affiliation>Bioprocess Engineering Laboratory, Department of Process and Environmental Engineering, University of Oulu, P, O, Box 4300, Oulu, FI-90014, Finland. juho.jarvinen@oulu.fi.</nlm:affiliation><country xml:lang="fr">Finlande</country><wicri:regionArea>Bioprocess Engineering Laboratory, Department of Process and Environmental Engineering, University of Oulu, P, O, Box 4300, Oulu, FI-90014</wicri:regionArea></affiliation></author><author><name sortKey="Taskila, Sanna" sort="Taskila, Sanna" uniqKey="Taskila S" first="Sanna" last="Taskila">Sanna Taskila</name></author><author><name sortKey="Isom Ki, Ritva" sort="Isom Ki, Ritva" uniqKey="Isom Ki R" first="Ritva" last="Isom Ki">Ritva Isom Ki</name></author><author><name sortKey="Ojamo, Heikki" sort="Ojamo, Heikki" uniqKey="Ojamo H" first="Heikki" last="Ojamo">Heikki Ojamo</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:23190610</idno><idno type="pmid">23190610</idno><idno type="doi">10.1186/2191-0855-2-62</idno><idno type="pmc">PMC3549895</idno><idno type="wicri:Area/Main/Corpus">000391</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000391</idno><idno type="wicri:Area/Main/Curation">000391</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000391</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Screening of white-rot fungi manganese peroxidases: a comparison between the specific activities of the enzyme from different native producers.</title><author><name sortKey="J Rvinen, Juho" sort="J Rvinen, Juho" uniqKey="J Rvinen J" first="Juho" last="J Rvinen">Juho J Rvinen</name><affiliation wicri:level="1"><nlm:affiliation>Bioprocess Engineering Laboratory, Department of Process and Environmental Engineering, University of Oulu, P, O, Box 4300, Oulu, FI-90014, Finland. juho.jarvinen@oulu.fi.</nlm:affiliation><country xml:lang="fr">Finlande</country><wicri:regionArea>Bioprocess Engineering Laboratory, Department of Process and Environmental Engineering, University of Oulu, P, O, Box 4300, Oulu, FI-90014</wicri:regionArea></affiliation></author><author><name sortKey="Taskila, Sanna" sort="Taskila, Sanna" uniqKey="Taskila S" first="Sanna" last="Taskila">Sanna Taskila</name></author><author><name sortKey="Isom Ki, Ritva" sort="Isom Ki, Ritva" uniqKey="Isom Ki R" first="Ritva" last="Isom Ki">Ritva Isom Ki</name></author><author><name sortKey="Ojamo, Heikki" sort="Ojamo, Heikki" uniqKey="Ojamo H" first="Heikki" last="Ojamo">Heikki Ojamo</name></author></analytic><series><title level="j">AMB Express</title><idno type="eISSN">2191-0855</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"> In this study manganese peroxidase (MnP) enzymes from selected white-rot fungi were isolated and compared for potential future recombinant production. White-rot fungi were cultivated in small-scale in liquid media and a simplified process was established for the purification of extracellular enzymes.Five lignin degrading organisms were selected (Bjerkandera sp., Phanerochaete (P.) chrysosporium, Physisporinus (P.) rivulosus, Phlebia (P.) radiata and Phlebia sp. Nf b19) and studied for MnP production in small-scale. Extracellular MnP activity was followed and cultivations were harvested at proximity of the peak activity. The production of MnPs varied in different organisms but was clearly regulated by inducing liquid media components (Mn2+, veratryl alcohol and malonate). In total 8 different MnP isoforms were purified.Results of this study reinforce the conception that MnPs from distinct organisms differ substantially in their properties. Production of the extracellular enzyme in general did not reach a substantial level. This further suggests that these native producers are not suitable for industrial scale production of the enzyme. The highest specific activities were observed with MnPs from P. chrysosporium (200 U mg-1), Phlebia sp. Nf b19 (55 U mg-1) and P. rivulosus (89 U mg-1) and these MnPs are considered as the most potential candidates for further studies. The molecular weight of the purified MnPs was estimated to be between 45-50 kDa.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">23190610</PMID><DateCompleted><Year>2013</Year><Month>01</Month><Day>23</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2191-0855</ISSN><JournalIssue CitedMedium="Internet"><Volume>2</Volume><Issue>1</Issue><PubDate><Year>2012</Year><Month>Nov</Month><Day>29</Day></PubDate></JournalIssue><Title>AMB Express</Title><ISOAbbreviation>AMB Express</ISOAbbreviation></Journal><ArticleTitle>Screening of white-rot fungi manganese peroxidases: a comparison between the specific activities of the enzyme from different native producers.</ArticleTitle><Pagination><MedlinePgn>62</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1186/2191-0855-2-62</ELocationID><Abstract><AbstractText> In this study manganese peroxidase (MnP) enzymes from selected white-rot fungi were isolated and compared for potential future recombinant production. White-rot fungi were cultivated in small-scale in liquid media and a simplified process was established for the purification of extracellular enzymes.Five lignin degrading organisms were selected (Bjerkandera sp., Phanerochaete (P.) chrysosporium, Physisporinus (P.) rivulosus, Phlebia (P.) radiata and Phlebia sp. Nf b19) and studied for MnP production in small-scale. Extracellular MnP activity was followed and cultivations were harvested at proximity of the peak activity. The production of MnPs varied in different organisms but was clearly regulated by inducing liquid media components (Mn2+, veratryl alcohol and malonate). In total 8 different MnP isoforms were purified.Results of this study reinforce the conception that MnPs from distinct organisms differ substantially in their properties. Production of the extracellular enzyme in general did not reach a substantial level. This further suggests that these native producers are not suitable for industrial scale production of the enzyme. The highest specific activities were observed with MnPs from P. chrysosporium (200 U mg-1), Phlebia sp. Nf b19 (55 U mg-1) and P. rivulosus (89 U mg-1) and these MnPs are considered as the most potential candidates for further studies. The molecular weight of the purified MnPs was estimated to be between 45-50 kDa.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Järvinen</LastName><ForeName>Juho</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Bioprocess Engineering Laboratory, Department of Process and Environmental Engineering, University of Oulu, P, O, Box 4300, Oulu, FI-90014, Finland. juho.jarvinen@oulu.fi.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Taskila</LastName><ForeName>Sanna</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Isomäki</LastName><ForeName>Ritva</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Ojamo</LastName><ForeName>Heikki</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate 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