ArticleJournal of industrial microbiology & biotechnology2015
Expression and display of a novel thermostable esterase from Clostridium thermocellum on the surface of Bacillus subtilis using the CotB anchor protein.
Article in Journal of industrial microbiology & biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- Display of Lignin Peroxidase on the Surface of Bacillus subtilis.Applied biochemistry and biotechnology · 2024Article
- Surface display of the COE antigen of porcine epidemic diarrhoea virus on Bacillus subtilis spores.Microbial biotechnology · 2024Article
- Applications ofMicroorganisms · 2024Review
- Progress in research and application development of surface display technology using Bacillus subtilis spores.Applied microbiology and biotechnology · 2020Review
- Bacillus subtilis Spore Surface Display of Haloalkane Dehalogenase DhaA.Current microbiology · 2019Article
- Surface Display of Bacterial Laccase CotA on Escherichia coli Cells and its Application in Industrial Dye Decolorization.Molecular biotechnology · 2018Article
- Vaccine display on artificial bacterial spores enhances protective efficacy against Staphylococcus aureus infection.FEMS microbiology letters · 2018Article
- Conversion of xylan by recyclable spores of Bacillus subtilis displaying thermophilic enzymes.Microbial cell factories · 2017Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Esterases expressed in microbial hosts are commercially valuable, but their applications are limited due to high costs of production and harsh industrial processes involved. In this study, the esterase-DSM (from Clostridium thermocellum) was expressed and successfully displayed on the spore surface, and the spore-associated esterase was confirmed by western blot analysis and activity measurements. The optimal temperature and pH of spore surface-displayed DSM was 60 and 8.5 °C, respectively. It also demonstrates a broad temperature and pH optimum in the range of 50-70, 7-9.5 °C. The spore surface-displayed esterase-DSM retained 78, 68 % of its original activity after 5 h incubation at 60 and 70 °C, respectively, which was twofold greater activity than that of the purified DSM. The recombinant spores has high activity and stability in DMSO, which was 49 % higher than the retained activity of the purified DSM in DMSO (20 % v/v), and retained 65.2 % of activity after 7 h of incubation in DMSO (20 % v/v). However, the recombinant spores could retain 77 % activity after 3 rounds of recycling. These results suggest that enzyme displayed on the surface of the Bacillus subtilis spore could serve as an effective approach for enzyme immobilization.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.