ArticleApplied and environmental microbiology2013
Carbohydrate-binding module-cyclodextrin glycosyltransferase fusion enables efficient synthesis of 2-O-d-glucopyranosyl-l-ascorbic acid with soluble starch as the glycosyl donor.
Article in Applied and environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- α-Amylase: Its Structure, Molecular Modification, and Application in the Food Field.Foods (Basel, Switzerland) · 2026Review
- Biofilm-based biocatalysis for β-cyclodextrin production by the surface-display of β-cyclodextrin glycosyltransferase in Bacillus subtilis.Scientific reports · 2024Article
- Multidomain chimeric enzymes as a promising alternative for biocatalysts improvement: a minireview.Molecular biology reports · 2024Review
- Heterologous expression of 4α-glucanotransferase: overproduction and properties for industrial applications.World journal of microbiology & biotechnology · 2022Review
- Review
- Engineering of Cyclodextrin Glycosyltransferase Reveals pH-Regulated Mechanism of Enhanced Long-Chain Glycosylated Sophoricoside Specificity.Applied and environmental microbiology · 2020Article
- High production of genistein diglucoside derivative using cyclodextrin glycosyltransferase from Paenibacillus macerans.Journal of industrial microbiology & biotechnology · 2017Article
- Fusion of self-assembling amphipathic oligopeptides with cyclodextrin glycosyltransferase improves 2-O-D-glucopyranosyl-L-ascorbic acid synthesis with soluble starch as the glycosyl donor.Applied and environmental microbiology · 2014Article
- Iterative saturation mutagenesis of -6 subsite residues in cyclodextrin glycosyltransferase from Paenibacillus macerans to improve maltodextrin specificity for 2-O-D-glucopyranosyl-L-ascorbic acid synthesis.Applied and environmental microbiology · 2013Article
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7 authors at 2 institutions in 2 countries.
Funding
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Abstract
In this study, we achieved the efficient synthesis of 2-O-d-glucopyranosyl-l-ascorbic acid (AA-2G) from soluble starch by fusing a carbohydrate-binding module (CBM) from Alkalimonas amylolytica α-amylase (CBMAmy) to cyclodextrin glycosyltransferase (CGTase) from Paenibacillus macerans. One fusion enzyme, CGT-CBMAmy, was constructed by fusing the CBMAmy to the C-terminal region of CGTase, and the other fusion enzyme, CGTΔE-CBMAmy, was obtained by replacing the E domain of CGTase with CBMAmy. The two fusion enzymes were then used to synthesize AA-2G from soluble starch as a cheap and easily soluble glycosyl donor. Under the optimal conditions, the AA-2G yields produced using CGTΔE-CBMAmy and CGT-CBMAmy were 2.01 g/liter and 3.03 g/liter, respectively, which were 3.94- and 5.94-fold of the yield from the wild-type CGTase (0.51 g/liter). The reaction kinetics of the two fusion enzymes were analyzed and modeled to confirm the enhanced specificity toward soluble starch. It was also found that, compared to the wild-type CGTase, the two fusion enzymes had relatively high hydrolysis and disproportionation activities, factors that favor AA-2G synthesis. Finally, it was speculated that the enhancement of soluble starch specificity may be related to the changes of substrate binding ability and the substrate binding sites between the CBM and the starch granule.
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