Article3 Biotech2018
Optimization of the fermentation conditions for the mutant strain of β-cyclodextrin glycosyltransferase H167C to produce cyclodextrins.
Article in 3 Biotech, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed, 6 citations in OpenAlex.
- The synergistic effect of metal ions and amino acids on the fermentation of β-CGTase-producing statin DF257.3 Biotech · 2024Article
- Enhanced production of questin by marine-derived3 Biotech · 2020Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cyclodextrin glycosyltransferase (CGTase) was used to catalyze the conversion of starch into cyclodextrins (CD) in industry. Improving the activity of CGTase to produce more CD with relative low cost is intensely interesting and has drawn wide attention. Amino acid mutation of His167 into Cys significantly enhanced β-CGTase activity; however, optimization of culture conditions for β-CGTase-H167C remains unclear. To determine this, the medium and culture conditions for β-CGTase-H167C were optimized with response surface methodology. Maximum activity of β-CGTase-H167C was obtained with the medium containing 1.1% corn starch, 4.4% corn steep liquor, 1.1% peptone, 0.02% MgSO
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Registered trials
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