Multienzyme Coimmobilization on Triheterofunctional Supports.
Journal
Biomacromolecules
ISSN: 1526-4602
Titre abrégé: Biomacromolecules
Pays: United States
ID NLM: 100892849
Informations de publication
Date de publication:
13 02 2023
13 02 2023
Historique:
pubmed:
18
1
2023
medline:
15
2
2023
entrez:
17
1
2023
Statut:
ppublish
Résumé
Immobilized multienzyme systems are gaining momentum in applied biocatalysis; however, the coimmobilization of several enzymes on one carrier is still challenging. In this work, we exploited a heterofunctional support activated with three different chemical functionalities to immobilize a wide variety of different enzymes. This support is based on agarose microbeads activated with aldehyde, amino, and cobalt chelate moieties that allow a fast and irreversible immobilization of enzymes, enhancing the thermostability of most of the heterogeneous biocatalysts (up to 21-fold higher than the soluble one). Furthermore, this trifunctional support serves to efficiently coimmobilize a multienzyme system composed of an alcohol dehydrogenase, a reduced nicotinamide adenine dinucleotide (NADH) oxidase, and a catalase. The confined multienzymatic system demonstrates higher performance than its free counterpart, achieving a total turnover number (TTN) of 1 × 10
Identifiants
pubmed: 36649203
doi: 10.1021/acs.biomac.2c01364
pmc: PMC10018741
doi:
Substances chimiques
Enzymes, Immobilized
0
Aldehydes
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
929-942Références
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