ArticleMolecular biotechnology2023
Expression of a Copper Activated Xylanase in Yeast: Location of the His-Tag in the Protein Significantly Affects the Enzymatic Properties.
Article in Molecular biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 9 citations in OpenAlex.
- Production of Xylooligosaccharides (XOSs) with Anti-inflammatory and Prebiotic Activities Using Recombinant Endo-1,4-β-xylanases fromJournal of agricultural and food chemistry · 2026Article
- Engineering artificial cross-species promoters with different transcriptional strengths.Synthetic and systems biotechnology · 2025Article
- Characterization and structural analysis of a leucine aminopeptidase using site-directed mutagenesis.AMB Express · 2024Article
- Novel His-tag Variants for Insertion Inside Polypeptide Chain.ACS omega · 2024Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A copper activated xylanase produced by E. coli BL21 was expressed in Pichia pastoris using the pGAPZαB expression vector. Two recombinant GH11 xylanase forms were obtained (N-His-rXAn11 and N-C-His-rXAn11). The findings revealed that the two recombinant xylanases displayed different behaviors toward the copper. In the presence of 3-mM Cu
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