Article3 Biotech2017
Improved activity of β-cyclodextrin glycosyltransferase from Bacillus sp. N-227 via mutagenesis of the conserved residues.
Article in 3 Biotech, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 14 citations in OpenAlex.
- The synergistic effect of metal ions and amino acids on the fermentation of β-CGTase-producing statin DF257.3 Biotech · 2024Article
- Engineering of cyclodextrin glycosyltransferase improves the conversion efficiency of rebaudioside A to glucosylated steviol glycosides and increases the content of short-chain glycosylated steviol glycoside.Microbial cell factories · 2023Article
- Heterologous expression of cyclodextrin glycosyltransferase from3 Biotech · 2023Article
- Molecular cloning, and optimized production and characterization of recombinant cyclodextrin glucanotransferase from3 Biotech · 2022Article
- Heterologous expression of 4α-glucanotransferase: overproduction and properties for industrial applications.World journal of microbiology & biotechnology · 2022Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-Cyclodextrin glycosyltransferase (β-CGTase) belongs to the α-amylase family of enzymes and converts starch to cyclic oligosaccharides called β-cyclodextrins (β-CD). The β-CGTase from alkalophilic Bacillus sp. N-227 was separately mutagenized to give three site-directed β-CGTase mutants, Y127F, R254F and D355R, that showed enhanced cyclization activity towards a starch substrate from 1.64 to 2.1-folds. Kinetic studies indicate that the mutants had higher affinity towards the substrate than the wild type β-CGTase. The Y127F mutant had the highest affinity which was indicated by the lowest K
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Registered trials
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