Functionalized Poplar Powder as a Support Material for Immobilization of Enoate Reductase and a Cofactor Regeneration System.
Identifieur interne : 000953 ( Main/Exploration ); précédent : 000952; suivant : 000954Functionalized Poplar Powder as a Support Material for Immobilization of Enoate Reductase and a Cofactor Regeneration System.
Auteurs : Han Li [République populaire de Chine] ; Xiumei Cui [République populaire de Chine] ; Liangyu Zheng [République populaire de Chine]Source :
- Journal of microbiology and biotechnology [ 1738-8872 ] ; 2019.
Descripteurs français
- KwdFr :
- Coenzymes (métabolisme), Enzymes immobilisées (métabolisme), Glucose 6-phosphate dehydrogenase (métabolisme), Glutaraldéhyde (MeSH), Immobilisation (méthodes), Lignine (composition chimique), Oxidoreductases (métabolisme), Populus (composition chimique), Régénération (MeSH), Stabilité enzymatique (MeSH), Éthylènediamines (MeSH).
- MESH :
- composition chimique : Lignine, Populus.
- métabolisme : Coenzymes, Enzymes immobilisées, Glucose 6-phosphate dehydrogenase, Oxidoreductases.
- méthodes : Immobilisation.
- Glutaraldéhyde, Régénération, Stabilité enzymatique, Éthylènediamines.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Lignin.
- chemical , metabolism : Coenzymes, Enzymes, Immobilized, Glucosephosphate Dehydrogenase, Oxidoreductases.
- chemistry : Populus.
- methods : Immobilization.
- Enzyme Stability, Ethylenediamines, Glutaral, Regeneration.
Abstract
In this study, functionalized poplar powder (FPP) was used as a support material for the immobilization of enoate reductase (ER) and glucose-6-phosphate dehydrogenase (GDH) by covalent binding. Under optimal conditions, the immobilization efficiency of ER-FPP and GDH-FPP was 95.1% and 84.7%, and the activity recovery of ER and GDH was 47.5% and 37.8%, respectively. Scanning electron microscopy (SEM) and energy dispersive spectroscopy (EDS) analysis indicated that FPP was a suitable carrier for enzyme immobilization. ER-FPP and GDH-FPP exhibit excellent thermal stabilities and superior reusability. Especially, ER-FPP and GDH-FPP enable the continuous conversion of 4-(4-Methoxyphenyl)-3-buten-2-one with NAD+ recycling. While the immobilization strategies established here were simple and inexpensive, they exploited a new method for the immobilization and application of ER and its cofactor recycling system.
DOI: 10.4014/jmb.1811.11054
PubMed: 30954031
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<term>Ethylenediamines (MeSH)</term>
<term>Glucosephosphate Dehydrogenase (metabolism)</term>
<term>Glutaral (MeSH)</term>
<term>Immobilization (methods)</term>
<term>Lignin (chemistry)</term>
<term>Oxidoreductases (metabolism)</term>
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<term>Éthylènediamines (MeSH)</term>
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<term>Glucosephosphate Dehydrogenase</term>
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<term>Régénération</term>
<term>Stabilité enzymatique</term>
<term>Éthylènediamines</term>
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<front><div type="abstract" xml:lang="en">In this study, functionalized poplar powder (FPP) was used as a support material for the immobilization of enoate reductase (ER) and glucose-6-phosphate dehydrogenase (GDH) by covalent binding. Under optimal conditions, the immobilization efficiency of ER-FPP and GDH-FPP was 95.1% and 84.7%, and the activity recovery of ER and GDH was 47.5% and 37.8%, respectively. Scanning electron microscopy (SEM) and energy dispersive spectroscopy (EDS) analysis indicated that FPP was a suitable carrier for enzyme immobilization. ER-FPP and GDH-FPP exhibit excellent thermal stabilities and superior reusability. Especially, ER-FPP and GDH-FPP enable the continuous conversion of 4-(4-Methoxyphenyl)-3-buten-2-one with NAD<sup>+</sup>
recycling. While the immobilization strategies established here were simple and inexpensive, they exploited a new method for the immobilization and application of ER and its cofactor recycling system.</div>
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<Abstract><AbstractText>In this study, functionalized poplar powder (FPP) was used as a support material for the immobilization of enoate reductase (ER) and glucose-6-phosphate dehydrogenase (GDH) by covalent binding. Under optimal conditions, the immobilization efficiency of ER-FPP and GDH-FPP was 95.1% and 84.7%, and the activity recovery of ER and GDH was 47.5% and 37.8%, respectively. Scanning electron microscopy (SEM) and energy dispersive spectroscopy (EDS) analysis indicated that FPP was a suitable carrier for enzyme immobilization. ER-FPP and GDH-FPP exhibit excellent thermal stabilities and superior reusability. Especially, ER-FPP and GDH-FPP enable the continuous conversion of 4-(4-Methoxyphenyl)-3-buten-2-one with NAD<sup>+</sup>
recycling. While the immobilization strategies established here were simple and inexpensive, they exploited a new method for the immobilization and application of ER and its cofactor recycling system.</AbstractText>
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