ArticleMicrobial cell factories2016
Display of a β-mannanase and a chitosanase on the cell surface of Lactobacillus plantarum towards the development of whole-cell biocatalysts.
Article in Microbial cell factories, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 43 citations in OpenAlex.
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- Effective synthesis of high-content fructooligosaccharides in engineered Aspergillus niger.Microbial cell factories · 2024Article
- Expanding the genetic programmability of Lactiplantibacillus plantarum.Microbial biotechnology · 2024Review
- Oral or intranasal immunization with recombinant Lactobacillus plantarum displaying head domain of Swine Influenza A virus hemagglutinin protects mice from H1N1 virus.Microbial cell factories · 2022Article
- A temperature-induced chitosanase bacterial cell-surface display system for the efficient production of chitooligosaccharides.Biotechnology letters · 2021Article
- Efficient Secretion and Recombinant Production of a Lactobacillal α-amylase inFrontiers in microbiology · 2021Article
- Introduction of Modified BglBrick System inFrontiers in bioengineering and biotechnology · 2021Article
- Identification and characterization of a moonlighting protein-enolase for surface display in Streptococcus thermophilus.Microbial cell factories · 2020Article
- Cell Wall Anchoring of a Bacterial Chitosanase inInternational journal of molecular sciences · 2020Article
- Safety Aspects of Genetically Modified Lactic Acid Bacteria.Microorganisms · 2020Review
- Galactose to tagatose isomerization at moderate temperatures with high conversion and productivity.Nature communications · 2019Article
- Immobilization of β-Galactosidases on theCatalysts (Basel, Switzerland) · 2019Article
- Constitutive expression and cell-surface display of a bacterial β-mannanase in Lactobacillus plantarum.Microbial cell factories · 2019Article
- Screening for New Surface Anchoring Domains forFrontiers in microbiology · 2019Article
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12 authors at 3 institutions in 4 countries.
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Abstract
backgroundLactobacillus plantarum is considered as a potential cell factory because of its GRAS (generally recognized as safe) status and long history of use in food applications. Its possible applications include in situ delivery of proteins to a host, based on its ability to persist at mucosal surfaces of the human intestine, and the production of food-related enzymes. By displaying different enzymes on the surface of L. plantarum cells these could be used as whole-cell biocatalysts for the production of oligosaccharides. In this present study, we aimed to express and display a mannanase and a chitosanase on the cell surface of L. plantarum.
resultsManB, a mannanase from Bacillus licheniformis DSM13, and CsnA, a chitosanase from Bacillus subtilis ATCC 23857 were fused to different anchoring motifs of L. plantarum for covalent attachment to the cell surface, either via an N-terminal lipoprotein anchor (Lp_1261) or a C-terminal cell wall anchor (Lp_2578), and the resulting fusion proteins were expressed in L. plantarum WCFS1. The localization of the recombinant proteins on the bacterial cell surface was confirmed by flow cytometry and immunofluorescence microscopy. The highest mannanase and chitosanase activities obtained for displaying L. plantarum cells were 890 U and 1360 U g dry cell weight, respectively. In reactions with chitosan and galactomannans, L. plantarum CsnA- and ManB-displaying cells produced chito- and manno-oligosaccharides, respectively, as analyzed by high performance anion exchange chromatography (HPAEC) and mass spectrometry (MS). Surface-displayed ManB is able to break down galactomannan (LBG) into smaller manno-oligosaccharides, which can support growth of L. plantarum.
conclusionThis study shows that mannanolytic and chitinolytic enzymes can be anchored to the cell surface of L. plantarum in active forms. L. plantarum chitosanase- and mannanase-displaying cells should be of interest for the production of potentially 'prebiotic' oligosaccharides. This approach, with the enzyme of interest being displayed on the cell surface of a food-grade organism, may also be applied in production processes relevant for food industry.
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