A valuable peroxidase activity from the novel species Nonomuraea gerenzanensis growing on alkali lignin.
Identifieur interne : 000193 ( Main/Exploration ); précédent : 000192; suivant : 000194A valuable peroxidase activity from the novel species Nonomuraea gerenzanensis growing on alkali lignin.
Auteurs : Carmine Casciello [Italie] ; Fabio Tonin [Italie] ; Francesca Berini [Italie] ; Elisa Fasoli [Italie] ; Flavia Marinelli [Italie] ; Loredano Pollegioni [Italie] ; Elena Rosini [Italie]Source :
- Biotechnology reports (Amsterdam, Netherlands) [ 2215-017X ] ; 2017.
Abstract
Degradation of lignin constitutes a key step in processing biomass to become useful monomers but it remains challenging. Compared to fungi, bacteria are much less characterized with respect to their lignin metabolism, although it is reported that many soil bacteria, especially actinomycetes, attack and solubilize lignin. In this work, we screened 43 filamentous actinomycetes by assaying their activity on chemically different substrates including a soluble and semi-degraded lignin derivative (known as alkali lignin or Kraft lignin), and we discovered a novel and valuable peroxidase activity produced by the recently classified actinomycete Nonomuraea gerenzanensis. Compared to known fungal manganese and versatile peroxidases, the stability of N. gerenzanensis peroxidase activity at alkaline pHs and its thermostability are significantly higher. From a kinetic point of view, N. gerenzanensis peroxidase activity shows a Km for H2O2 similar to that of Phanerochaete chrysosporium and Bjerkandera enzymes and a lower affinity for Mn2+, whereas it differs from the six Pleurotus ostreatus manganese peroxidase isoenzymes described in the literature. Additionally, N. gerenzanensis peroxidase shows a remarkable dye-decolorizing activity that expands its substrate range and paves the way for an industrial use of this enzyme. These results confirm that by exploring new bacterial diversity, we may be able to discover and exploit alternative biological tools putatively involved in lignin modification and degradation.
DOI: 10.1016/j.btre.2016.12.005
PubMed: 28352563
PubMed Central: PMC5361131
Affiliations:
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Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano</wicri:regionArea><wicri:noRegion>20131 Milano</wicri:noRegion></affiliation></author><author><name sortKey="Tonin, Fabio" sort="Tonin, Fabio" uniqKey="Tonin F" first="Fabio" last="Tonin">Fabio Tonin</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano</wicri:regionArea><wicri:noRegion>20131 Milano</wicri:noRegion></affiliation></author><author><name sortKey="Berini, Francesca" sort="Berini, Francesca" uniqKey="Berini F" first="Francesca" last="Berini">Francesca Berini</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano</wicri:regionArea><wicri:noRegion>20131 Milano</wicri:noRegion></affiliation></author><author><name sortKey="Fasoli, Elisa" sort="Fasoli, Elisa" uniqKey="Fasoli E" first="Elisa" last="Fasoli">Elisa Fasoli</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, Materials and Chemical Engineering "Giulio Natta", Politecnico of Milano, via Mancinelli 7, 20131, Milano, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, Materials and Chemical Engineering "Giulio Natta", Politecnico of Milano, via Mancinelli 7, 20131, Milano</wicri:regionArea><wicri:noRegion>Milano</wicri:noRegion></affiliation></author><author><name sortKey="Marinelli, Flavia" sort="Marinelli, Flavia" uniqKey="Marinelli F" first="Flavia" last="Marinelli">Flavia Marinelli</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano</wicri:regionArea><wicri:noRegion>20131 Milano</wicri:noRegion></affiliation></author><author><name sortKey="Pollegioni, Loredano" sort="Pollegioni, Loredano" uniqKey="Pollegioni L" first="Loredano" last="Pollegioni">Loredano Pollegioni</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano</wicri:regionArea><wicri:noRegion>20131 Milano</wicri:noRegion></affiliation></author><author><name sortKey="Rosini, Elena" sort="Rosini, Elena" uniqKey="Rosini E" first="Elena" last="Rosini">Elena Rosini</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano</wicri:regionArea><wicri:noRegion>20131 Milano</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biotechnology reports (Amsterdam, Netherlands)</title><idno type="ISSN">2215-017X</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Degradation of lignin constitutes a key step in processing biomass to become useful monomers but it remains challenging. Compared to fungi, bacteria are much less characterized with respect to their lignin metabolism, although it is reported that many soil bacteria, especially actinomycetes, attack and solubilize lignin. In this work, we screened 43 filamentous actinomycetes by assaying their activity on chemically different substrates including a soluble and semi-degraded lignin derivative (known as alkali lignin or Kraft lignin), and we discovered a novel and valuable peroxidase activity produced by the recently classified actinomycete <i>Nonomuraea gerenzanensis.</i> Compared to known fungal manganese and versatile peroxidases, the stability of <i>N. gerenzanensis</i> peroxidase activity at alkaline pHs and its thermostability are significantly higher. From a kinetic point of view, <i>N. gerenzanensis</i> peroxidase activity shows a <i>K</i><sub>m</sub> for H<sub>2</sub>O<sub>2</sub> similar to that of <i>Phanerochaete chrysosporium</i> and <i>Bjerkandera</i> enzymes and a lower affinity for Mn<sup>2+</sup>, whereas it differs from the six <i>Pleurotus ostreatus</i> manganese peroxidase isoenzymes described in the literature. Additionally, <i>N. gerenzanensis</i> peroxidase shows a remarkable dye-decolorizing activity that expands its substrate range and paves the way for an industrial use of this enzyme. These results confirm that by exploring new bacterial diversity, we may be able to discover and exploit alternative biological tools putatively involved in lignin modification and degradation.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">28352563</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">2215-017X</ISSN><JournalIssue CitedMedium="Print"><Volume>13</Volume><PubDate><Year>2017</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Biotechnology reports (Amsterdam, Netherlands)</Title><ISOAbbreviation>Biotechnol Rep (Amst)</ISOAbbreviation></Journal><ArticleTitle>A valuable peroxidase activity from the novel species <i>Nonomuraea gerenzanensis</i> growing on alkali lignin.</ArticleTitle><Pagination><MedlinePgn>49-57</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.btre.2016.12.005</ELocationID><Abstract><AbstractText>Degradation of lignin constitutes a key step in processing biomass to become useful monomers but it remains challenging. Compared to fungi, bacteria are much less characterized with respect to their lignin metabolism, although it is reported that many soil bacteria, especially actinomycetes, attack and solubilize lignin. In this work, we screened 43 filamentous actinomycetes by assaying their activity on chemically different substrates including a soluble and semi-degraded lignin derivative (known as alkali lignin or Kraft lignin), and we discovered a novel and valuable peroxidase activity produced by the recently classified actinomycete <i>Nonomuraea gerenzanensis.</i> Compared to known fungal manganese and versatile peroxidases, the stability of <i>N. gerenzanensis</i> peroxidase activity at alkaline pHs and its thermostability are significantly higher. From a kinetic point of view, <i>N. gerenzanensis</i> peroxidase activity shows a <i>K</i><sub>m</sub> for H<sub>2</sub>O<sub>2</sub> similar to that of <i>Phanerochaete chrysosporium</i> and <i>Bjerkandera</i> enzymes and a lower affinity for Mn<sup>2+</sup>, whereas it differs from the six <i>Pleurotus ostreatus</i> manganese peroxidase isoenzymes described in the literature. Additionally, <i>N. gerenzanensis</i> peroxidase shows a remarkable dye-decolorizing activity that expands its substrate range and paves the way for an industrial use of this enzyme. These results confirm that by exploring new bacterial diversity, we may be able to discover and exploit alternative biological tools putatively involved in lignin modification and degradation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Casciello</LastName><ForeName>Carmine</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tonin</LastName><ForeName>Fabio</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Berini</LastName><ForeName>Francesca</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fasoli</LastName><ForeName>Elisa</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Materials and Chemical Engineering "Giulio Natta", Politecnico of Milano, via Mancinelli 7, 20131, Milano, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Marinelli</LastName><ForeName>Flavia</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pollegioni</LastName><ForeName>Loredano</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rosini</LastName><ForeName>Elena</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano, Italy.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>01</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biotechnol Rep (Amst)</MedlineTA><NlmUniqueID>101637426</NlmUniqueID><ISSNLinking>2215-017X</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">2,4-DCP, 2,4-dichlorophenol</Keyword><Keyword MajorTopicYN="N">2,6-DMP, 2,6-dimethoxyphenol</Keyword><Keyword MajorTopicYN="N">ABTS, 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid)</Keyword><Keyword MajorTopicYN="N">Alkali lignin</Keyword><Keyword MajorTopicYN="N">DyP, dye decolorizing peroxidase</Keyword><Keyword MajorTopicYN="N">Filamentous actinomycetes</Keyword><Keyword MajorTopicYN="N">Kraft lignin</Keyword><Keyword MajorTopicYN="N">LiP, lignin peroxidase</Keyword><Keyword MajorTopicYN="N">MAM, mannitol agar medium</Keyword><Keyword MajorTopicYN="N">MM-L, minimal salt medium plus lignin</Keyword><Keyword MajorTopicYN="N">MnP, manganese peroxidase</Keyword><Keyword MajorTopicYN="N">Nonomuraea gerenzanensis</Keyword><Keyword MajorTopicYN="N">Peroxidases</Keyword><Keyword MajorTopicYN="N">RB5, reactive black 5</Keyword><Keyword MajorTopicYN="N">RBBR, remazol brilliant blue R</Keyword><Keyword MajorTopicYN="N">VP, versatile peroxidase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>08</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>12</Month><Day>07</Day></PubMedPubDate><PubMedPubDate 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