Vault packaged enzyme mediated degradation of amino-aromatic energetic compounds.
Identifieur interne : 000043 ( Main/Corpus ); précédent : 000042; suivant : 000044Vault packaged enzyme mediated degradation of amino-aromatic energetic compounds.
Auteurs : Anjali G. Lothe ; Shashank Singh Kalra ; Meng Wang ; Elizabeth Erin Mack ; Claudia Walecka-Hutchison ; Valerie A. Kickhoefer ; Leonard H. Rome ; Shaily MahendraSource :
- Chemosphere [ 1879-1298 ] ; 2020.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Environmental Pollutants, Organic Chemicals.
- chemistry : Nanoparticles.
- metabolism : Phanerochaete.
- Biodegradation, Environmental, Peroxidases.
Abstract
Amino-aromatic compounds, 2-amino-4-nitrotoluene (ANT), and 2,4-diaminotoluene (DAT) are carcinogens and environmentally persistent pollutants. In this study, we investigated their degradation by natural manganese peroxidase (nMnP) derived from Phanerochaete chrysosporium and recombinant manganese peroxidase packaged in vaults (vMnP). Encapsulation of manganese peroxidase (MnP) in ribonucleoprotein nanoparticle cages, called vaults, was achieved by creating recombinant vaults in yeast Pichia pastoris. Vault packaging increased the stability of MnP by locally sequestering multiple copies of the enzyme. Within 96 h, both vMnP and nMnP catalyzed over 72% removal of ANT in-vitro, which indicates that vault packaging did not limit substrate diffusion. It was observed that vMnP was more efficient than nMnP and P. chrysosporium for the catalysis of target contaminants. Only 57% of ANT was degraded by P. chrysosporium even when MnP activity reached about 480 U L-1 in cultures. At 1.5 U L-1 initial activity, vMnP achieved 38% of ANT and 51% of DAT degradation, whereas even 2.7 times higher activity of nMnP showed insignificant biodegradation of both compounds. These results imply that due to protection by vault cages, vMnP has lower inactivation rates. Thus, it works effectively at lower dosage for a longer duration compared to nMnP without requiring frequent replenishment. Collectively, these results indicate that fungal enzymes packaged in vault nanoparticles are more stable and active, and they would be effective in biodegradation of energetic compounds in industrial processes, waste treatment, and contaminated environments.
DOI: 10.1016/j.chemosphere.2019.125117
PubMed: 31655399
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Lothe</name><affiliation><nlm:affiliation>Civil and Environmental Engineering, University of California, Los Angeles, CA, 90095, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Kalra, Shashank Singh" sort="Kalra, Shashank Singh" uniqKey="Kalra S" first="Shashank Singh" last="Kalra">Shashank Singh Kalra</name><affiliation><nlm:affiliation>Civil and Environmental Engineering, University of California, Los Angeles, CA, 90095, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Wang, Meng" sort="Wang, Meng" uniqKey="Wang M" first="Meng" last="Wang">Meng Wang</name><affiliation><nlm:affiliation>Civil and Environmental Engineering, University of California, Los Angeles, CA, 90095, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Mack, Elizabeth Erin" sort="Mack, Elizabeth Erin" uniqKey="Mack E" first="Elizabeth Erin" last="Mack">Elizabeth Erin Mack</name><affiliation><nlm:affiliation>Corteva Environmental Remediation, Corteva Agriscience, Newark, DE, 19711, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Walecka Hutchison, Claudia" sort="Walecka Hutchison, Claudia" uniqKey="Walecka Hutchison C" first="Claudia" last="Walecka-Hutchison">Claudia Walecka-Hutchison</name><affiliation><nlm:affiliation>Environmental Remediation and Restoration, The Dow Chemical Company, Midland, MI, 48674, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Kickhoefer, Valerie A" sort="Kickhoefer, Valerie A" uniqKey="Kickhoefer V" first="Valerie A" last="Kickhoefer">Valerie A. Kickhoefer</name><affiliation><nlm:affiliation>Vault Nano, Inc., Los Angeles, CA, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Rome, Leonard H" sort="Rome, Leonard H" uniqKey="Rome L" first="Leonard H" last="Rome">Leonard H. Rome</name><affiliation><nlm:affiliation>Biological Chemistry, UCLA David Geffen School of Medicine, Los Angeles, CA, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Mahendra, Shaily" sort="Mahendra, Shaily" uniqKey="Mahendra S" first="Shaily" last="Mahendra">Shaily Mahendra</name><affiliation><nlm:affiliation>Civil and Environmental Engineering, University of California, Los Angeles, CA, 90095, United States. 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Lothe</name><affiliation><nlm:affiliation>Civil and Environmental Engineering, University of California, Los Angeles, CA, 90095, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Kalra, Shashank Singh" sort="Kalra, Shashank Singh" uniqKey="Kalra S" first="Shashank Singh" last="Kalra">Shashank Singh Kalra</name><affiliation><nlm:affiliation>Civil and Environmental Engineering, University of California, Los Angeles, CA, 90095, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Wang, Meng" sort="Wang, Meng" uniqKey="Wang M" first="Meng" last="Wang">Meng Wang</name><affiliation><nlm:affiliation>Civil and Environmental Engineering, University of California, Los Angeles, CA, 90095, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Mack, Elizabeth Erin" sort="Mack, Elizabeth Erin" uniqKey="Mack E" first="Elizabeth Erin" last="Mack">Elizabeth Erin Mack</name><affiliation><nlm:affiliation>Corteva Environmental Remediation, Corteva Agriscience, Newark, DE, 19711, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Walecka Hutchison, Claudia" sort="Walecka Hutchison, Claudia" uniqKey="Walecka Hutchison C" first="Claudia" last="Walecka-Hutchison">Claudia Walecka-Hutchison</name><affiliation><nlm:affiliation>Environmental Remediation and Restoration, The Dow Chemical Company, Midland, MI, 48674, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Kickhoefer, Valerie A" sort="Kickhoefer, Valerie A" uniqKey="Kickhoefer V" first="Valerie A" last="Kickhoefer">Valerie A. Kickhoefer</name><affiliation><nlm:affiliation>Vault Nano, Inc., Los Angeles, CA, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Rome, Leonard H" sort="Rome, Leonard H" uniqKey="Rome L" first="Leonard H" last="Rome">Leonard H. Rome</name><affiliation><nlm:affiliation>Biological Chemistry, UCLA David Geffen School of Medicine, Los Angeles, CA, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Mahendra, Shaily" sort="Mahendra, Shaily" uniqKey="Mahendra S" first="Shaily" last="Mahendra">Shaily Mahendra</name><affiliation><nlm:affiliation>Civil and Environmental Engineering, University of California, Los Angeles, CA, 90095, United States. Electronic address: mahendra@seas.ucla.edu.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Chemosphere</title><idno type="eISSN">1879-1298</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biodegradation, Environmental (MeSH)</term><term>Environmental Pollutants (metabolism)</term><term>Nanoparticles (chemistry)</term><term>Organic Chemicals (metabolism)</term><term>Peroxidases (MeSH)</term><term>Phanerochaete (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Environmental Pollutants</term><term>Organic Chemicals</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nanoparticles</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biodegradation, Environmental</term><term>Peroxidases</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Amino-aromatic compounds, 2-amino-4-nitrotoluene (ANT), and 2,4-diaminotoluene (DAT) are carcinogens and environmentally persistent pollutants. In this study, we investigated their degradation by natural manganese peroxidase (nMnP) derived from Phanerochaete chrysosporium and recombinant manganese peroxidase packaged in vaults (vMnP). Encapsulation of manganese peroxidase (MnP) in ribonucleoprotein nanoparticle cages, called vaults, was achieved by creating recombinant vaults in yeast Pichia pastoris. Vault packaging increased the stability of MnP by locally sequestering multiple copies of the enzyme. Within 96 h, both vMnP and nMnP catalyzed over 72% removal of ANT in-vitro, which indicates that vault packaging did not limit substrate diffusion. It was observed that vMnP was more efficient than nMnP and P. chrysosporium for the catalysis of target contaminants. Only 57% of ANT was degraded by P. chrysosporium even when MnP activity reached about 480 U L<sup>-1</sup> in cultures. At 1.5 U L<sup>-1</sup> initial activity, vMnP achieved 38% of ANT and 51% of DAT degradation, whereas even 2.7 times higher activity of nMnP showed insignificant biodegradation of both compounds. These results imply that due to protection by vault cages, vMnP has lower inactivation rates. Thus, it works effectively at lower dosage for a longer duration compared to nMnP without requiring frequent replenishment. Collectively, these results indicate that fungal enzymes packaged in vault nanoparticles are more stable and active, and they would be effective in biodegradation of energetic compounds in industrial processes, waste treatment, and contaminated environments.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Curated" Owner="NLM"><PMID Version="1">31655399</PMID><DateCompleted><Year>2020</Year><Month>02</Month><Day>18</Day></DateCompleted><DateRevised><Year>2020</Year><Month>02</Month><Day>18</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-1298</ISSN><JournalIssue CitedMedium="Internet"><Volume>242</Volume><PubDate><Year>2020</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Chemosphere</Title><ISOAbbreviation>Chemosphere</ISOAbbreviation></Journal><ArticleTitle>Vault packaged enzyme mediated degradation of amino-aromatic energetic compounds.</ArticleTitle><Pagination><MedlinePgn>125117</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0045-6535(19)32356-2</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.chemosphere.2019.125117</ELocationID><Abstract><AbstractText>Amino-aromatic compounds, 2-amino-4-nitrotoluene (ANT), and 2,4-diaminotoluene (DAT) are carcinogens and environmentally persistent pollutants. In this study, we investigated their degradation by natural manganese peroxidase (nMnP) derived from Phanerochaete chrysosporium and recombinant manganese peroxidase packaged in vaults (vMnP). Encapsulation of manganese peroxidase (MnP) in ribonucleoprotein nanoparticle cages, called vaults, was achieved by creating recombinant vaults in yeast Pichia pastoris. Vault packaging increased the stability of MnP by locally sequestering multiple copies of the enzyme. Within 96 h, both vMnP and nMnP catalyzed over 72% removal of ANT in-vitro, which indicates that vault packaging did not limit substrate diffusion. It was observed that vMnP was more efficient than nMnP and P. chrysosporium for the catalysis of target contaminants. Only 57% of ANT was degraded by P. chrysosporium even when MnP activity reached about 480 U L<sup>-1</sup> in cultures. At 1.5 U L<sup>-1</sup> initial activity, vMnP achieved 38% of ANT and 51% of DAT degradation, whereas even 2.7 times higher activity of nMnP showed insignificant biodegradation of both compounds. These results imply that due to protection by vault cages, vMnP has lower inactivation rates. Thus, it works effectively at lower dosage for a longer duration compared to nMnP without requiring frequent replenishment. Collectively, these results indicate that fungal enzymes packaged in vault nanoparticles are more stable and active, and they would be effective in biodegradation of energetic compounds in industrial processes, waste treatment, and contaminated environments.</AbstractText><CopyrightInformation>Copyright © 2019 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lothe</LastName><ForeName>Anjali G</ForeName><Initials>AG</Initials><AffiliationInfo><Affiliation>Civil and Environmental Engineering, University of California, Los Angeles, CA, 90095, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kalra</LastName><ForeName>Shashank Singh</ForeName><Initials>SS</Initials><AffiliationInfo><Affiliation>Civil and Environmental Engineering, University of California, Los Angeles, CA, 90095, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Meng</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Civil and Environmental Engineering, University of California, Los Angeles, CA, 90095, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mack</LastName><ForeName>Elizabeth Erin</ForeName><Initials>EE</Initials><AffiliationInfo><Affiliation>Corteva Environmental Remediation, Corteva Agriscience, Newark, DE, 19711, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Walecka-Hutchison</LastName><ForeName>Claudia</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Environmental Remediation and Restoration, The Dow Chemical Company, Midland, MI, 48674, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kickhoefer</LastName><ForeName>Valerie A</ForeName><Initials>VA</Initials><AffiliationInfo><Affiliation>Vault Nano, Inc., Los Angeles, CA, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rome</LastName><ForeName>Leonard H</ForeName><Initials>LH</Initials><AffiliationInfo><Affiliation>Biological Chemistry, UCLA David Geffen School of Medicine, Los Angeles, CA, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mahendra</LastName><ForeName>Shaily</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Civil and Environmental Engineering, University of California, Los Angeles, CA, 90095, United States. Electronic address: mahendra@seas.ucla.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>10</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Chemosphere</MedlineTA><NlmUniqueID>0320657</NlmUniqueID><ISSNLinking>0045-6535</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004785">Environmental Pollutants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009930">Organic Chemicals</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001673" MajorTopicYN="Y">Biodegradation, Environmental</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004785" MajorTopicYN="N">Environmental Pollutants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053758" MajorTopicYN="N">Nanoparticles</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009930" MajorTopicYN="N">Organic Chemicals</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Bioremediation</Keyword><Keyword MajorTopicYN="N">Biotransformation</Keyword><Keyword MajorTopicYN="N">Dynamic structure</Keyword><Keyword MajorTopicYN="N">Immobilization</Keyword><Keyword MajorTopicYN="N">Ligninolytic</Keyword><Keyword MajorTopicYN="N">Nanocages</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>05</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>10</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>10</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>10</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>2</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>10</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31655399</ArticleId><ArticleId IdType="pii">S0045-6535(19)32356-2</ArticleId><ArticleId IdType="doi">10.1016/j.chemosphere.2019.125117</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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