ArticleJournal of industrial microbiology & biotechnology2017
Site-saturation mutagenesis of mutant L-asparaginase II signal peptide hydrophobic region for improved excretion of cyclodextrin glucanotransferase.
Article in Journal of industrial microbiology & biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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
3 citing papers in PubMed, 10 citations in OpenAlex.
- Toward the Development of a Biosimilar Variant of Glucarpidase (Carboxypeptidase G2): Secretory Production, Optimization, and Immobilization.Molecular biotechnology · 2026Article
- Heterologous expression of 4α-glucanotransferase: overproduction and properties for industrial applications.World journal of microbiology & biotechnology · 2022Review
- Highly Expressed Soluble Recombinant Anti-GFP VHHs inFrontiers in molecular biosciences · 2022Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
The excretion of cyclodextrin glucanotransferase (CGTase) into the culture medium offers significant advantages over cytoplasmic expression. However, the limitation of Escherichia coli is its inability to excrete high amount of CGTase outside the cells. In this study, modification of the hydrophobic region of the N1R3 signal peptide using site-saturation mutagenesis improved the excretion of CGTase. Signal peptide mutants designated M9F, V10L and A15Y enhanced the excretion of CGTase three-fold and demonstrated two-fold higher secretion rate than the wild type. However, high secretion rate of these mutants was non-productive for recombinant protein production because it caused up to a seven-fold increase in cell death compared to the wild type. Our results indicated that the excretion of CGTase is highly dependent on hydrophobicity, secondary conformation and the type and position of amino acids at the region boundary and core segment of the h-region.
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