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Single stage bi-substrate transglycosylation reaction for the synthesis of ascorbic acid 2 glucoside using immobilized α-glucosidase.
- Source :
-
Biocatalysis & Biotransformation . Sep2024, p1-13. 13p. 8 Illustrations. - Publication Year :
- 2024
-
Abstract
- AbstractAlpha glucosidases are multifunctional glycoside hydrolases with hydrolysis and transglycosylation ability. It can be utilized for the glycosidic bond synthesis or glycosylation of Ascorbic acid/Vitamin C to its stable analogue, Ascorbic acid 2 glucoside (AA2G), a compound with wide applications in cosmetics and pharma. The application of α-glucosidases for industrial scale transglycosylation is limited due to the low transglycosylation yield of free enzymes. Enzyme immobilization techniques could enable the development of efficient, reusable catalysts. Only a few glycoside hydrolases have been studied in immobilized form for transglycosylation reactions, and α-glucosidases are probably the least explored in this form. Transglycosylation activity of immobilized α-glucosidase from <italic>Aspergillus carbonarius</italic> BTCF 5 was studied for AA2G synthesis, where different immobilization techniques like calcium alginate encapsulation, adsorption on chitosan beads, covalent cross-linking on magnetic nanoparticles, and cross-linked enzyme aggregates (CLEA) were employed for the immobilization. The immobilization yield of calcium alginate encapsulated enzyme, enzyme immobilized on Fe-MNP support, enzyme immobilized on chitosan beads and as CLEA were 107%, 99%, 46% and 486%, respectively. CLEA was identified as the best immobilization technique for this bi-substrate reaction due to the high immobilization yield and activity retention (30% activity retained after 5 consecutive cycles). Enzyme immobilization increased the transglycosylation activity by 38%, yielding 118 mM AA2G against 72 mM by the free enzyme. This indicates the potential of immobilized α-glucosidase as a catalyst for synthesizing AA2G at an industrial scale. [ABSTRACT FROM AUTHOR]
- Subjects :
- *GLYCOSIDASES
*VITAMIN C
*MAGNETIC nanoparticles
*ENZYMES
*CATALYSTS
*GLUCOSIDASES
Subjects
Details
- Language :
- English
- ISSN :
- 10242422
- Database :
- Academic Search Index
- Journal :
- Biocatalysis & Biotransformation
- Publication Type :
- Academic Journal
- Accession number :
- 179570860
- Full Text :
- https://doi.org/10.1080/10242422.2024.2400074