Directly covalent immobilization of Candida antarctica lipase B on oxidized aspen powder by introducing poly‑lysines: An economical approach to improve enzyme performance.
Identifieur interne : 000A23 ( Main/Exploration ); précédent : 000A22; suivant : 000A24Directly covalent immobilization of Candida antarctica lipase B on oxidized aspen powder by introducing poly‑lysines: An economical approach to improve enzyme performance.
Auteurs : Xiaoxue Zhou [République populaire de Chine] ; Han Li [République populaire de Chine] ; Liangyu Zheng [République populaire de Chine]Source :
- International journal of biological macromolecules [ 1879-0003 ] ; 2019.
Descripteurs français
- KwdFr :
- Biomasse (MeSH), Enzymes immobilisées (composition chimique), Enzymes immobilisées (métabolisme), Oxydoréduction (MeSH), Polylysine (composition chimique), Populus (composition chimique), Poudres (MeSH), Protéines fongiques (composition chimique), Protéines fongiques (métabolisme), Stabilité enzymatique (MeSH), Triacylglycerol lipase (composition chimique), Triacylglycerol lipase (métabolisme).
- MESH :
- composition chimique : Enzymes immobilisées, Polylysine, Populus, Protéines fongiques, Triacylglycerol lipase.
- métabolisme : Enzymes immobilisées, Protéines fongiques, Triacylglycerol lipase.
- Biomasse, Oxydoréduction, Poudres, Stabilité enzymatique.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Enzymes, Immobilized, Fungal Proteins, Lipase, Polylysine.
- chemical , metabolism : Enzymes, Immobilized, Fungal Proteins, Lipase.
- chemistry : Populus.
- Biomass, Enzyme Stability, Oxidation-Reduction, Powders.
Abstract
In our previous study, we could achieve high soluble expression of Candida antarctica lipase B (CalB) in E. coli by fusion poly‑amino acid tags on CalB (pCalB). Herein, we are surprised to find that pCalB can be easily and directly covalent binding on a simply oxidized aspen powder (OAP) by the aid of poly‑lysine tags. Under the optimal conditions, 72.9 ± 3.6% of the total protein could be immobilized, and the activity recovery of immobilized pCalB (pCalB-OAP) was 98.9 ± 3.8%. The analysis of scanning electron microscopy (SEM) and Fourier transform infrared spectroscopy (FTIR) indicated that OAP was a suitable carrier for enzyme immobilization. The immobilized pCalB-OAP could exhibit excellent thermal stabilities, and it retained a residual activity of 58.4 ± 2.8% at 55 °C, whereas only 21.2 ± 2.2% of its initial activity for free pCalB was observed. And it could also display a nice tolerance for the changes of pH environment, compared with that of free pCalB. The results that pCalB-OAP could retained 73.6 ± 2.9% of their initial activity in (R, S)-NEMPAME hydrolysis after the tenth cycles, suggested that pCalB-OAP could be effectively recycled. The immobilization strategies established here were simple and inexpensive.
DOI: 10.1016/j.ijbiomac.2019.04.096
PubMed: 30986456
Affiliations:
Links toward previous steps (curation, corpus...)
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Electronic address: zhengliangyu@jlu.edu.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Sciences, Jilin University, Changchun 130012</wicri:regionArea><placeName><settlement type="city">Changchun</settlement><region type="province">Jilin</region><region type="groupement">Dongbei</region></placeName><orgName type="university">Université de Jilin</orgName><placeName><settlement type="city">Changchun</settlement><region type="province">Jilin</region></placeName></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>Biomass (MeSH)</term><term>Enzyme Stability (MeSH)</term><term>Enzymes, Immobilized (chemistry)</term><term>Enzymes, Immobilized (metabolism)</term><term>Fungal Proteins (chemistry)</term><term>Fungal Proteins (metabolism)</term><term>Lipase (chemistry)</term><term>Lipase (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Polylysine (chemistry)</term><term>Populus (chemistry)</term><term>Powders (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Biomasse (MeSH)</term><term>Enzymes immobilisées (composition chimique)</term><term>Enzymes immobilisées (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Polylysine (composition chimique)</term><term>Populus (composition chimique)</term><term>Poudres (MeSH)</term><term>Protéines fongiques (composition chimique)</term><term>Protéines fongiques (métabolisme)</term><term>Stabilité enzymatique (MeSH)</term><term>Triacylglycerol lipase (composition chimique)</term><term>Triacylglycerol lipase (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Enzymes, Immobilized</term><term>Fungal Proteins</term><term>Lipase</term><term>Polylysine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Enzymes, Immobilized</term><term>Fungal Proteins</term><term>Lipase</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Enzymes immobilisées</term><term>Polylysine</term><term>Populus</term><term>Protéines fongiques</term><term>Triacylglycerol lipase</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Enzymes immobilisées</term><term>Protéines fongiques</term><term>Triacylglycerol lipase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biomass</term><term>Enzyme Stability</term><term>Oxidation-Reduction</term><term>Powders</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biomasse</term><term>Oxydoréduction</term><term>Poudres</term><term>Stabilité enzymatique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In our previous study, we could achieve high soluble expression of Candida antarctica lipase B (CalB) in E. coli by fusion poly‑amino acid tags on CalB (pCalB). Herein, we are surprised to find that pCalB can be easily and directly covalent binding on a simply oxidized aspen powder (OAP) by the aid of poly‑lysine tags. Under the optimal conditions, 72.9 ± 3.6% of the total protein could be immobilized, and the activity recovery of immobilized pCalB (pCalB-OAP) was 98.9 ± 3.8%. The analysis of scanning electron microscopy (SEM) and Fourier transform infrared spectroscopy (FTIR) indicated that OAP was a suitable carrier for enzyme immobilization. The immobilized pCalB-OAP could exhibit excellent thermal stabilities, and it retained a residual activity of 58.4 ± 2.8% at 55 °C, whereas only 21.2 ± 2.2% of its initial activity for free pCalB was observed. And it could also display a nice tolerance for the changes of pH environment, compared with that of free pCalB. The results that pCalB-OAP could retained 73.6 ± 2.9% of their initial activity in (R, S)-NEMPAME hydrolysis after the tenth cycles, suggested that pCalB-OAP could be effectively recycled. The immobilization strategies established here were simple and inexpensive.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30986456</PMID><DateCompleted><Year>2019</Year><Month>12</Month><Day>20</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0003</ISSN><JournalIssue CitedMedium="Internet"><Volume>133</Volume><PubDate><Year>2019</Year><Month>Jul</Month><Day>15</Day></PubDate></JournalIssue><Title>International journal of biological macromolecules</Title><ISOAbbreviation>Int J Biol Macromol</ISOAbbreviation></Journal><ArticleTitle>Directly covalent immobilization of Candida antarctica lipase B on oxidized aspen powder by introducing poly‑lysines: An economical approach to improve enzyme performance.</ArticleTitle><Pagination><MedlinePgn>226-234</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0141-8130(18)36221-4</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ijbiomac.2019.04.096</ELocationID><Abstract><AbstractText>In our previous study, we could achieve high soluble expression of Candida antarctica lipase B (CalB) in E. coli by fusion poly‑amino acid tags on CalB (pCalB). Herein, we are surprised to find that pCalB can be easily and directly covalent binding on a simply oxidized aspen powder (OAP) by the aid of poly‑lysine tags. Under the optimal conditions, 72.9 ± 3.6% of the total protein could be immobilized, and the activity recovery of immobilized pCalB (pCalB-OAP) was 98.9 ± 3.8%. The analysis of scanning electron microscopy (SEM) and Fourier transform infrared spectroscopy (FTIR) indicated that OAP was a suitable carrier for enzyme immobilization. The immobilized pCalB-OAP could exhibit excellent thermal stabilities, and it retained a residual activity of 58.4 ± 2.8% at 55 °C, whereas only 21.2 ± 2.2% of its initial activity for free pCalB was observed. And it could also display a nice tolerance for the changes of pH environment, compared with that of free pCalB. The results that pCalB-OAP could retained 73.6 ± 2.9% of their initial activity in (R, S)-NEMPAME hydrolysis after the tenth cycles, suggested that pCalB-OAP could be effectively recycled. The immobilization strategies established here were simple and inexpensive.</AbstractText><CopyrightInformation>Copyright © 2019 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhou</LastName><ForeName>Xiaoxue</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Sciences, Jilin University, Changchun 130012, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Han</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Sciences, Jilin University, Changchun 130012, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zheng</LastName><ForeName>Liangyu</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Sciences, Jilin University, Changchun 130012, People's Republic of China. Electronic address: zhengliangyu@jlu.edu.cn.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>04</Month><Day>13</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="D004800">Enzymes, Immobilized</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011208">Powders</NameOfSubstance></Chemical><Chemical><RegistryNumber>25104-18-1</RegistryNumber><NameOfSubstance UI="D011107">Polylysine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.1.3</RegistryNumber><NameOfSubstance UI="D008049">Lipase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.1.3</RegistryNumber><NameOfSubstance UI="C431349">lipase B, Candida antarctica</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D018533" MajorTopicYN="Y">Biomass</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004800" MajorTopicYN="N">Enzymes, Immobilized</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008049" MajorTopicYN="N">Lipase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011107" MajorTopicYN="N">Polylysine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011208" MajorTopicYN="N">Powders</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Aspen powder</Keyword><Keyword MajorTopicYN="N">Candida antarctica lipase B</Keyword><Keyword MajorTopicYN="N">Poly‑lysine tag</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>11</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>04</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>04</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>4</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>12</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>4</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30986456</ArticleId><ArticleId IdType="pii">S0141-8130(18)36221-4</ArticleId><ArticleId IdType="doi">10.1016/j.ijbiomac.2019.04.096</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country><region><li>Dongbei</li><li>Jilin</li></region><settlement><li>Changchun</li></settlement><orgName><li>Université de Jilin</li></orgName></list><tree><country name="République populaire de Chine"><region name="Jilin"><name sortKey="Zhou, Xiaoxue" sort="Zhou, Xiaoxue" uniqKey="Zhou X" first="Xiaoxue" last="Zhou">Xiaoxue Zhou</name></region><name sortKey="Li, Han" sort="Li, Han" uniqKey="Li H" first="Han" last="Li">Han Li</name><name sortKey="Zheng, Liangyu" sort="Zheng, Liangyu" uniqKey="Zheng L" first="Liangyu" last="Zheng">Liangyu Zheng</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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