Serveur d'exploration sur le peuplier

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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 : 000954

Functionalized 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 :

RBID : pubmed:30954031

Descripteurs français

English descriptors

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:


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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>
<term>Populus (chemistry)</term>
<term>Regeneration (MeSH)</term>
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<term>Glutaraldéhyde (MeSH)</term>
<term>Immobilisation (méthodes)</term>
<term>Lignine (composition chimique)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Populus (composition chimique)</term>
<term>Régénération (MeSH)</term>
<term>Stabilité enzymatique (MeSH)</term>
<term>Éthylènediamines (MeSH)</term>
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<term>Lignin</term>
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<term>Coenzymes</term>
<term>Enzymes, Immobilized</term>
<term>Glucosephosphate Dehydrogenase</term>
<term>Oxidoreductases</term>
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<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
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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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