ArticleCurrent microbiology2015
Display of fungi xylanase on Escherichia coli cell surface and use of the enzyme in xylan biodegradation.
Article in Current microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 22 citations in OpenAlex.
- Expression of phenylalanine ammonia lyase as an intracellularly free and extracellularly cell surface-immobilized enzyme on a gut microbe as a live biotherapeutic for phenylketonuria.Science China. Life sciences · 2023Article
- Engineering mesophilic GH11 xylanase fromFrontiers in bioengineering and biotechnology · 2022Article
- Whole-cell display of Pyrococcus horikoshii glutamate decarboxylase in Escherichia coli for high-titer extracellular gamma-aminobutyric acid production.Journal of industrial microbiology & biotechnology · 2021Article
- BeQuIK (Biosensor Engineered Quorum Induced Killing): designer bacteria for destroying recalcitrant biofilms.Microbial biotechnology · 2020Article
- Engineering E. coli cell surface in order to develop a one-step purification method for recombinant proteins.AMB Express · 2018Article
- Manganese and cobalt recovery by surface display of metal binding peptide on various loops of OmpC in Escherichia coli.Journal of industrial microbiology & biotechnology · 2018Article
- Whole cell biocatalysts: essential workers from Nature to the industry.Microbial biotechnology · 2017Review
- Heterologous expression of antigenic peptides in Bacillus subtilis biofilms.Microbial cell factories · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cell surface display technique allows expression of target proteins or peptides on microbial cell surface by fusing an appropriate protein as an anchoring motif. Herein, we constructed an Escherichia coli-based whole-cell biocatalyst displaying Thermomyces lanuginosus DSM 5826 xylanase (XynA) on the cell surface and endowed the E. coli cells with the ability to degrade xylan. The XynA was fused in frame to the C-terminus of Lpp-OmpA fusion previously shown to direct various other heterologous proteins to E. coli cell surface. The expressed Lpp-OmpA-XynA fusion protein has a molecular weight of approximately 37 kDa, which was confirmed by SDS-PAGE and Western blot analysis. The enzyme activity of the surface-displayed xylanase showed clear halo around the colony. The XynA-displaying E. coli-based whole-cell biocatalyst xylanase activity was mainly detected with whole cells by determination of activity. The XynA-displaying E. coli-based whole-cell biocatalyst showed highest XynA activity at pH 6.2 and 65 °C, respectively. These results suggest that E. coli, which displayed the xylanase on its surface, could be used as a whole-cell biocatalyst in xylooligosaccharide production.
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