Recombinant lignin peroxidase-catalyzed decolorization of melanin using in-situ generated H2O2 for application in whitening cosmetics.
Identifieur interne : 000056 ( Main/Exploration ); précédent : 000055; suivant : 000057Recombinant lignin peroxidase-catalyzed decolorization of melanin using in-situ generated H2O2 for application in whitening cosmetics.
Auteurs : Ho Joon Sung [Corée du Sud] ; Mohd Faheem Khan [Corée du Sud] ; Yong Hwan Kim [Corée du Sud]Source :
- International journal of biological macromolecules [ 1879-0003 ] ; 2019.
Descripteurs français
- KwdFr :
- Biocatalyse (MeSH), Conformation des protéines (MeSH), Cosmétiques (métabolisme), Couleur (MeSH), Glucose oxidase (composition chimique), Glucose oxidase (métabolisme), Modèles moléculaires (MeSH), Mélanines (métabolisme), Peroxidases (composition chimique), Peroxidases (métabolisme), Peroxyde d'hydrogène (métabolisme), Protéines recombinantes (composition chimique), Protéines recombinantes (métabolisme).
- MESH :
- composition chimique : Glucose oxidase, Peroxidases, Protéines recombinantes.
- métabolisme : Cosmétiques, Glucose oxidase, Mélanines, Peroxidases, Peroxyde d'hydrogène, Protéines recombinantes.
- Biocatalyse, Conformation des protéines, Couleur, Modèles moléculaires.
English descriptors
- KwdEn :
- Biocatalysis (MeSH), Color (MeSH), Cosmetics (metabolism), Glucose Oxidase (chemistry), Glucose Oxidase (metabolism), Hydrogen Peroxide (metabolism), Melanins (metabolism), Models, Molecular (MeSH), Peroxidases (chemistry), Peroxidases (metabolism), Protein Conformation (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism).
- MESH :
- chemical , chemistry : Glucose Oxidase, Peroxidases, Recombinant Proteins.
- chemical , metabolism : Cosmetics, Glucose Oxidase, Hydrogen Peroxide, Melanins, Peroxidases, Recombinant Proteins.
- Biocatalysis, Color, Models, Molecular, Protein Conformation.
Abstract
Lignin peroxidase has high potential as ingredient in skin whitening cosmetics due to its high redox potential to oxidize recalcitrant melanin. Currently crude mixtures of lignin peroxidase from fungal fermentation are usually applied to cosmetics due to the intrinsic difficulties of expression and purification. However, the present study focused on heterologous expression and purification of lignin peroxidase isozyme H8 (LiPH8) from Phanerochaete chrysosporium and was further used for melanin decolorization. Results revealed that the optimum pH for melanin decolorization using LiPH8 was obtained at pH 4.0. The intermittent feeding of hydrogen peroxide (H2O2) was effectively elevating melanin decolorization efficiency up to 73%, since excessive H2O2 inactivated LiPH8. For cosmetic application, intermittent feeding of H2O2 is not feasible, thus glucose oxidase (GOx) from Aspergillus niger was employed for in-situ generation of H2O2. By optimizing the GOx and glucose concentrations, a melanin decolorization efficiency up to 63.3 ± 2.4% was obtained within 1 h and continued to 84.0 ± 1.8% in 8 h. Conclusively, lignin peroxidase-catalyzed decolorization of melanin with in-situ generated H2O2 revealed a promising approach for whitening cosmetics applications.
DOI: 10.1016/j.ijbiomac.2019.06.026
PubMed: 31175901
Affiliations:
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Electronic address: metalkim@unist.ac.kr.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), 50, UNIST-gil, Ulsan 44919</wicri:regionArea><wicri:noRegion>Ulsan 44919</wicri:noRegion></affiliation></author></analytic><series><title level="j">International journal of biological macromolecules</title><idno type="eISSN">1879-0003</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biocatalysis (MeSH)</term><term>Color (MeSH)</term><term>Cosmetics (metabolism)</term><term>Glucose Oxidase (chemistry)</term><term>Glucose Oxidase (metabolism)</term><term>Hydrogen Peroxide (metabolism)</term><term>Melanins (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Peroxidases (chemistry)</term><term>Peroxidases (metabolism)</term><term>Protein Conformation (MeSH)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Biocatalyse (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cosmétiques (métabolisme)</term><term>Couleur (MeSH)</term><term>Glucose oxidase (composition chimique)</term><term>Glucose oxidase (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Mélanines (métabolisme)</term><term>Peroxidases (composition chimique)</term><term>Peroxidases (métabolisme)</term><term>Peroxyde d'hydrogène (métabolisme)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glucose Oxidase</term><term>Peroxidases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cosmetics</term><term>Glucose Oxidase</term><term>Hydrogen Peroxide</term><term>Melanins</term><term>Peroxidases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glucose oxidase</term><term>Peroxidases</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cosmétiques</term><term>Glucose oxidase</term><term>Mélanines</term><term>Peroxidases</term><term>Peroxyde d'hydrogène</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biocatalysis</term><term>Color</term><term>Models, Molecular</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biocatalyse</term><term>Conformation des protéines</term><term>Couleur</term><term>Modèles moléculaires</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lignin peroxidase has high potential as ingredient in skin whitening cosmetics due to its high redox potential to oxidize recalcitrant melanin. Currently crude mixtures of lignin peroxidase from fungal fermentation are usually applied to cosmetics due to the intrinsic difficulties of expression and purification. However, the present study focused on heterologous expression and purification of lignin peroxidase isozyme H8 (LiPH8) from Phanerochaete chrysosporium and was further used for melanin decolorization. Results revealed that the optimum pH for melanin decolorization using LiPH8 was obtained at pH 4.0. The intermittent feeding of hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) was effectively elevating melanin decolorization efficiency up to 73%, since excessive H<sub>2</sub>O<sub>2</sub> inactivated LiPH8. For cosmetic application, intermittent feeding of H<sub>2</sub>O<sub>2</sub> is not feasible, thus glucose oxidase (GOx) from Aspergillus niger was employed for in-situ generation of H<sub>2</sub>O<sub>2</sub>. By optimizing the GOx and glucose concentrations, a melanin decolorization efficiency up to 63.3 ± 2.4% was obtained within 1 h and continued to 84.0 ± 1.8% in 8 h. Conclusively, lignin peroxidase-catalyzed decolorization of melanin with in-situ generated H<sub>2</sub>O<sub>2</sub> revealed a promising approach for whitening cosmetics applications.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31175901</PMID><DateCompleted><Year>2019</Year><Month>12</Month><Day>31</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>31</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0003</ISSN><JournalIssue CitedMedium="Internet"><Volume>136</Volume><PubDate><Year>2019</Year><Month>Sep</Month><Day>01</Day></PubDate></JournalIssue><Title>International journal of biological macromolecules</Title><ISOAbbreviation>Int J Biol Macromol</ISOAbbreviation></Journal><ArticleTitle>Recombinant lignin peroxidase-catalyzed decolorization of melanin using in-situ generated H<sub>2</sub>O<sub>2</sub> for application in whitening cosmetics.</ArticleTitle><Pagination><MedlinePgn>20-26</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0141-8130(19)32309-8</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ijbiomac.2019.06.026</ELocationID><Abstract><AbstractText>Lignin peroxidase has high potential as ingredient in skin whitening cosmetics due to its high redox potential to oxidize recalcitrant melanin. Currently crude mixtures of lignin peroxidase from fungal fermentation are usually applied to cosmetics due to the intrinsic difficulties of expression and purification. However, the present study focused on heterologous expression and purification of lignin peroxidase isozyme H8 (LiPH8) from Phanerochaete chrysosporium and was further used for melanin decolorization. Results revealed that the optimum pH for melanin decolorization using LiPH8 was obtained at pH 4.0. The intermittent feeding of hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) was effectively elevating melanin decolorization efficiency up to 73%, since excessive H<sub>2</sub>O<sub>2</sub> inactivated LiPH8. For cosmetic application, intermittent feeding of H<sub>2</sub>O<sub>2</sub> is not feasible, thus glucose oxidase (GOx) from Aspergillus niger was employed for in-situ generation of H<sub>2</sub>O<sub>2</sub>. By optimizing the GOx and glucose concentrations, a melanin decolorization efficiency up to 63.3 ± 2.4% was obtained within 1 h and continued to 84.0 ± 1.8% in 8 h. Conclusively, lignin peroxidase-catalyzed decolorization of melanin with in-situ generated H<sub>2</sub>O<sub>2</sub> revealed a promising approach for whitening cosmetics applications.</AbstractText><CopyrightInformation>Copyright © 2019 The Authors. Published by Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sung</LastName><ForeName>Ho Joon</ForeName><Initials>HJ</Initials><AffiliationInfo><Affiliation>School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), 50, UNIST-gil, Ulsan 44919, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Khan</LastName><ForeName>Mohd Faheem</ForeName><Initials>MF</Initials><AffiliationInfo><Affiliation>School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), 50, UNIST-gil, Ulsan 44919, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Yong Hwan</ForeName><Initials>YH</Initials><AffiliationInfo><Affiliation>School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), 50, UNIST-gil, Ulsan 44919, Republic of Korea. Electronic address: metalkim@unist.ac.kr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>06</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Int J Biol Macromol</MedlineTA><NlmUniqueID>7909578</NlmUniqueID><ISSNLinking>0141-8130</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003358">Cosmetics</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008543">Melanins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.4</RegistryNumber><NameOfSubstance UI="D005949">Glucose Oxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D055162" MajorTopicYN="Y">Biocatalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003116" MajorTopicYN="N">Color</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003358" MajorTopicYN="N">Cosmetics</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005949" MajorTopicYN="N">Glucose Oxidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008543" MajorTopicYN="N">Melanins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Glucose oxidase</Keyword><Keyword MajorTopicYN="N">Lignin peroxidase</Keyword><Keyword MajorTopicYN="N">Melanin decolorization</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>03</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>05</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>06</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>6</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>1</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>6</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31175901</ArticleId><ArticleId IdType="pii">S0141-8130(19)32309-8</ArticleId><ArticleId IdType="doi">10.1016/j.ijbiomac.2019.06.026</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Corée du Sud</li></country></list><tree><country name="Corée du Sud"><noRegion><name sortKey="Sung, Ho Joon" sort="Sung, Ho Joon" uniqKey="Sung H" first="Ho Joon" last="Sung">Ho Joon Sung</name></noRegion><name sortKey="Khan, Mohd Faheem" sort="Khan, Mohd Faheem" uniqKey="Khan M" first="Mohd Faheem" last="Khan">Mohd Faheem Khan</name><name sortKey="Kim, Yong Hwan" sort="Kim, Yong Hwan" uniqKey="Kim Y" first="Yong Hwan" last="Kim">Yong Hwan Kim</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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