Alcohol dehydrogenases from Scheffersomyces stipitis involved in the detoxification of aldehyde inhibitors derived from lignocellulosic biomass conversion.
Identifieur interne : 001892 ( Main/Exploration ); précédent : 001891; suivant : 001893Alcohol dehydrogenases from Scheffersomyces stipitis involved in the detoxification of aldehyde inhibitors derived from lignocellulosic biomass conversion.
Auteurs : Menggen Ma [République populaire de Chine] ; Xu Wang ; Xiaoping Zhang ; Xianxian ZhaoSource :
- Applied microbiology and biotechnology [ 1432-0614 ] ; 2013.
Descripteurs français
- KwdFr :
- Alcohol dehydrogenase (composition chimique), Alcohol dehydrogenase (génétique), Alcohol dehydrogenase (métabolisme), Alignement de séquences (MeSH), Biocarburants (analyse), Cinétique (MeSH), Données de séquences moléculaires (MeSH), Furfural (analogues et dérivés), Furfural (métabolisme), Lignine (métabolisme), NADP (métabolisme), Phylogenèse (MeSH), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Saccharomycetales (classification), Saccharomycetales (composition chimique), Saccharomycetales (enzymologie), Saccharomycetales (génétique), Spécificité du substrat (MeSH), Stabilité enzymatique (MeSH), Séquence d'acides aminés (MeSH), Éthanol (métabolisme).
- MESH :
- analogues et dérivés : Furfural.
- analyse : Biocarburants.
- composition chimique : Alcohol dehydrogenase, Protéines fongiques, Saccharomycetales.
- enzymologie : Saccharomycetales.
- génétique : Alcohol dehydrogenase, Protéines fongiques, Saccharomycetales.
- métabolisme : Alcohol dehydrogenase, Furfural, Lignine, NADP, Protéines fongiques, Éthanol.
- Alignement de séquences, Cinétique, Données de séquences moléculaires, Phylogenèse, Spécificité du substrat, Stabilité enzymatique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Alcohol Dehydrogenase (chemistry), Alcohol Dehydrogenase (genetics), Alcohol Dehydrogenase (metabolism), Amino Acid Sequence (MeSH), Biofuels (analysis), Enzyme Stability (MeSH), Ethanol (metabolism), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Furaldehyde (analogs & derivatives), Furaldehyde (metabolism), Kinetics (MeSH), Lignin (metabolism), Molecular Sequence Data (MeSH), NADP (metabolism), Phylogeny (MeSH), Saccharomycetales (chemistry), Saccharomycetales (classification), Saccharomycetales (enzymology), Saccharomycetales (genetics), Sequence Alignment (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , analogs & derivatives : Furaldehyde.
- chemical , analysis : Biofuels.
- chemical , chemistry : Alcohol Dehydrogenase, Fungal Proteins.
- chemical , genetics : Alcohol Dehydrogenase, Fungal Proteins.
- chemical , metabolism : Alcohol Dehydrogenase, Ethanol, Fungal Proteins, Furaldehyde, Lignin, NADP.
- chemistry : Saccharomycetales.
- classification : Saccharomycetales.
- enzymology : Saccharomycetales.
- genetics : Saccharomycetales.
- Amino Acid Sequence, Enzyme Stability, Kinetics, Molecular Sequence Data, Phylogeny, Sequence Alignment, Substrate Specificity.
Abstract
Aldehyde inhibitors such as furfural and 5-hydroxymethylfurfural (HMF) are generated from biomass pretreatment. Scheffersomyces stipitis is able to reduce furfural and HMF to less toxic furanmethanol and furan-2,5-dimethanol; however, the enzymes involved in the reductive reaction still remain unknown. In this study, transcription responses of two known and five putative alcohol dehydrogenase genes from S. stipitis were analyzed under furfural and HMF stress conditions. All the seven alcohol dehydrogenase genes were also cloned and overexpressed for their activity analyses. Our results indicate that transcriptions of SsADH4 and SsADH6 were highly induced under furfural and HMF stress conditions, and the proteins encoded by them exhibited NADH- and/or NADPH-dependent activities for furfural and HMF reduction, respectively. For furfural reduction, NADH-dependent activity was also observed in SsAdh1p and NAD(P)H-dependent activities were also observed in SsAdh5p and SsAdh7p. For HMF reduction, NADPH-dependent activities were also observed in SsAdh5p and SsAdh7p. SsAdh4p displayed the highest NADPH-dependent specific activity and catalytic efficiency for reduction of both furfural and HMF among the seven alcohol dehydrogenases. Enzyme activities of all SsADH proteins were more stable under acidic condition. For most SsADH proteins, the optimum temperature for enzyme activities was 30 °C and more than 50 % enzyme activities remained at 60 °C. Reduction activities of formaldehyde, acetaldehyde, isovaleraldehyde, benzaldehyde, and phenylacetaldehyde were also observed in some SsADH proteins. Our results indicate that multiple alcohol dehydrogenases in S. stipitis are involved in the detoxification of aldehyde inhibitors derived from lignocellulosic biomass conversion.
DOI: 10.1007/s00253-013-5110-8
PubMed: 23912116
Affiliations:
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detoxification of aldehyde inhibitors derived from lignocellulosic biomass conversion.</title><author><name sortKey="Ma, Menggen" sort="Ma, Menggen" uniqKey="Ma M" first="Menggen" last="Ma">Menggen Ma</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Ecological and Environmental Sciences, Sichuan Agricultural University, No. 211 Huimin Road, Wenjiang, Sichuan, 611130, People's Republic of China. mgen23@hotmail.com</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Institute of Ecological and Environmental Sciences, Sichuan Agricultural University, No. 211 Huimin Road, Wenjiang, Sichuan, 611130</wicri:regionArea><wicri:noRegion>611130</wicri:noRegion></affiliation></author><author><name sortKey="Wang, Xu" sort="Wang, Xu" uniqKey="Wang X" first="Xu" last="Wang">Xu Wang</name></author><author><name sortKey="Zhang, Xiaoping" sort="Zhang, Xiaoping" uniqKey="Zhang X" first="Xiaoping" last="Zhang">Xiaoping 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aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Aldehyde inhibitors such as furfural and 5-hydroxymethylfurfural (HMF) are generated from biomass pretreatment. Scheffersomyces stipitis is able to reduce furfural and HMF to less toxic furanmethanol and furan-2,5-dimethanol; however, the enzymes involved in the reductive reaction still remain unknown. In this study, transcription responses of two known and five putative alcohol dehydrogenase genes from S. stipitis were analyzed under furfural and HMF stress conditions. All the seven alcohol dehydrogenase genes were also cloned and overexpressed for their activity analyses. Our results indicate that transcriptions of SsADH4 and SsADH6 were highly induced under furfural and HMF stress conditions, and the proteins encoded by them exhibited NADH- and/or NADPH-dependent activities for furfural and HMF reduction, respectively. For furfural reduction, NADH-dependent activity was also observed in SsAdh1p and NAD(P)H-dependent activities were also observed in SsAdh5p and SsAdh7p. For HMF reduction, NADPH-dependent activities were also observed in SsAdh5p and SsAdh7p. SsAdh4p displayed the highest NADPH-dependent specific activity and catalytic efficiency for reduction of both furfural and HMF among the seven alcohol dehydrogenases. Enzyme activities of all SsADH proteins were more stable under acidic condition. For most SsADH proteins, the optimum temperature for enzyme activities was 30 °C and more than 50 % enzyme activities remained at 60 °C. Reduction activities of formaldehyde, acetaldehyde, isovaleraldehyde, benzaldehyde, and phenylacetaldehyde were also observed in some SsADH proteins. Our results indicate that multiple alcohol dehydrogenases in S. stipitis are involved in the detoxification of aldehyde inhibitors derived from lignocellulosic biomass conversion. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23912116</PMID><DateCompleted><Year>2014</Year><Month>03</Month><Day>10</Day></DateCompleted><DateRevised><Year>2013</Year><Month>08</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-0614</ISSN><JournalIssue CitedMedium="Internet"><Volume>97</Volume><Issue>18</Issue><PubDate><Year>2013</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Applied microbiology and biotechnology</Title><ISOAbbreviation>Appl Microbiol Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Alcohol dehydrogenases from Scheffersomyces stipitis involved in the detoxification of aldehyde inhibitors derived from lignocellulosic biomass conversion.</ArticleTitle><Pagination><MedlinePgn>8411-25</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00253-013-5110-8</ELocationID><Abstract><AbstractText>Aldehyde inhibitors such as furfural and 5-hydroxymethylfurfural (HMF) are generated from biomass pretreatment. Scheffersomyces stipitis is able to reduce furfural and HMF to less toxic furanmethanol and furan-2,5-dimethanol; however, the enzymes involved in the reductive reaction still remain unknown. In this study, transcription responses of two known and five putative alcohol dehydrogenase genes from S. stipitis were analyzed under furfural and HMF stress conditions. All the seven alcohol dehydrogenase genes were also cloned and overexpressed for their activity analyses. Our results indicate that transcriptions of SsADH4 and SsADH6 were highly induced under furfural and HMF stress conditions, and the proteins encoded by them exhibited NADH- and/or NADPH-dependent activities for furfural and HMF reduction, respectively. For furfural reduction, NADH-dependent activity was also observed in SsAdh1p and NAD(P)H-dependent activities were also observed in SsAdh5p and SsAdh7p. For HMF reduction, NADPH-dependent activities were also observed in SsAdh5p and SsAdh7p. SsAdh4p displayed the highest NADPH-dependent specific activity and catalytic efficiency for reduction of both furfural and HMF among the seven alcohol dehydrogenases. Enzyme activities of all SsADH proteins were more stable under acidic condition. For most SsADH proteins, the optimum temperature for enzyme activities was 30 °C and more than 50 % enzyme activities remained at 60 °C. Reduction activities of formaldehyde, acetaldehyde, isovaleraldehyde, benzaldehyde, and phenylacetaldehyde were also observed in some SsADH proteins. Our results indicate that multiple alcohol dehydrogenases in S. stipitis are involved in the detoxification of aldehyde inhibitors derived from lignocellulosic biomass conversion. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ma</LastName><ForeName>Menggen</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institute of Ecological and Environmental Sciences, Sichuan Agricultural University, No. 211 Huimin Road, Wenjiang, Sichuan, 611130, People's Republic of China. mgen23@hotmail.com</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Xu</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Xiaoping</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Zhao</LastName><ForeName>Xianxian</ForeName><Initials>X</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>08</Month><Day>04</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Appl Microbiol Biotechnol</MedlineTA><NlmUniqueID>8406612</NlmUniqueID><ISSNLinking>0175-7598</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D056804">Biofuels</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>11132-73-3</RegistryNumber><NameOfSubstance UI="C036909">lignocellulose</NameOfSubstance></Chemical><Chemical><RegistryNumber>3K9958V90M</RegistryNumber><NameOfSubstance UI="D000431">Ethanol</NameOfSubstance></Chemical><Chemical><RegistryNumber>53-59-8</RegistryNumber><NameOfSubstance UI="D009249">NADP</NameOfSubstance></Chemical><Chemical><RegistryNumber>70ETD81LF0</RegistryNumber><NameOfSubstance UI="C008046">5-hydroxymethylfurfural</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>DJ1HGI319P</RegistryNumber><NameOfSubstance UI="D005662">Furaldehyde</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.1</RegistryNumber><NameOfSubstance UI="D000426">Alcohol Dehydrogenase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000426" MajorTopicYN="N">Alcohol Dehydrogenase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D056804" MajorTopicYN="N">Biofuels</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000431" MajorTopicYN="N">Ethanol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005662" MajorTopicYN="N">Furaldehyde</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009249" MajorTopicYN="N">NADP</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004718" MajorTopicYN="N">Saccharomycetales</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>05</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>07</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>07</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>8</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>8</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>3</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23912116</ArticleId><ArticleId IdType="doi">10.1007/s00253-013-5110-8</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><noCountry><name sortKey="Wang, Xu" sort="Wang, Xu" uniqKey="Wang X" first="Xu" last="Wang">Xu Wang</name><name sortKey="Zhang, Xiaoping" sort="Zhang, Xiaoping" uniqKey="Zhang X" first="Xiaoping" last="Zhang">Xiaoping Zhang</name><name sortKey="Zhao, Xianxian" sort="Zhao, Xianxian" uniqKey="Zhao X" first="Xianxian" last="Zhao">Xianxian Zhao</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Ma, Menggen" 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