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Spatially sequential co-immobilization of phosphorylases in tiny environments and its application in the synthesis of glucosyl glycerol.
- Source :
-
International journal of biological macromolecules [Int J Biol Macromol] 2024 Nov; Vol. 279 (Pt 2), pp. 135139. Date of Electronic Publication: 2024 Aug 27. - Publication Year :
- 2024
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Abstract
- 2-O-(α-d-glucopyranosyl)-sn-glycerol (2-αGG) has been applied in the food industry due to its numerous physiological benefits. The synthesis of 2-αGG can be achieved through a cascade catalytic reaction involving sucrose phosphorylase (SP) and 2-O-α-glucosylglycerol phosphorylase (GGP). However, the low substrate transfer rates between free enzymes have hindered the efficiency of 2-αGG synthesis. To address this issue, a novel technology was developed to prepare sequential multi-enzyme nanoflowers via chemical crosslinking and protein assembly, thus overcoming diffusion limitations. Specifically, spatially sequential co-immobilized enzymes, referred to as SP-GGP@Cap, were created through the targeted assembly of Bifidobacterium adolescentis SP and Marinobacter adhaerens GGP on Ca <superscript>2+</superscript> . This assembly was facilitated by the spontaneous protein reaction between SpyTag and SpyCatcher. Compared to free SP-GGP, SP-GGP@Cap demonstrated improved thermal and pH stability. Moreover, SP-GGP@Cap enhanced the biosynthesis of 2-αGG, achieving a relative concentration of 98 %. Additionally, it retained the ability to catalyze the substrate to yield 61 % relative concentration of 2-αGG even after ten cycles of recycling. This study presents a strategy for the spatially sequential co-immobilization of multiple enzymes in a confined environment and provides an exceptional biocatalyst for the potential industrial production of 2-αGG.<br />Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.<br /> (Copyright © 2024 Elsevier B.V. All rights reserved.)
- Subjects :
- Glucosides chemistry
Glucosides biosynthesis
Glucosides metabolism
Glucosyltransferases metabolism
Glucosyltransferases chemistry
Bifidobacterium adolescentis enzymology
Hydrogen-Ion Concentration
Phosphorylases metabolism
Phosphorylases chemistry
Enzyme Stability
Temperature
Enzymes, Immobilized metabolism
Enzymes, Immobilized chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1879-0003
- Volume :
- 279
- Issue :
- Pt 2
- Database :
- MEDLINE
- Journal :
- International journal of biological macromolecules
- Publication Type :
- Academic Journal
- Accession number :
- 39208907
- Full Text :
- https://doi.org/10.1016/j.ijbiomac.2024.135139