ArticleWorld journal of microbiology & biotechnology2017
Purification, characterization, and overexpression of an endo-1,4-β-mannanase from thermotolerant Bacillus sp. SWU60.
Article in World journal of microbiology & biotechnology, 2017. 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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Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- Harnessing magnetic cross-linked cell aggregates (CLCAs) for cost-effective preparation of Konjac mannan-oligosaccharide.Microbial cell factories · 2025Article
- Research and application progress of microbial β-mannanases: a mini-review.World journal of microbiology & biotechnology · 2024Review
- High NaCl concentrations induce the resistance to thermal denaturation of an extremely halotolerant (salt-activated) β-mannanase from Bacillus velezensis H1.World journal of microbiology & biotechnology · 2023Article
- Complete Genome Sequences of Mannanase-ProducingMicrobiology resource announcements · 2022Article
- Proteomic perspectives on thermotolerant microbes: an updated review.Molecular biology reports · 2022Review
- Applications of Microbial β-Mannanases.Frontiers in bioengineering and biotechnology · 2020Review
- Characterization and high-efficiency secreted expression in Bacillus subtilis of a thermo-alkaline β-mannanase from an alkaliphilic Bacillus clausii strain S10.Microbial cell factories · 2018Article
- Biochemical characterization of a thermostable endomannanase/endoglucanase from Dictyoglomus turgidum.Extremophiles : life under extreme conditions · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endo-β-1,4-mannanases are important catalytic agents in several industries. The enzymes randomly cleave the β-1,4-linkage in the mannan backbone and release short β-1,4-mannooligosaccharides and mannose. In the present study, mannanase (ManS2) from thermotolerant Bacillus sp. SWU60 was purified, characterized, and its gene was cloned and overexpressed in Escherichia coli. ManS2 was purified from culture filtrate (300 ml) by using hydrophobic, ion-exchange, and size-exclusive liquid chromatography. The apparent molecular mass was 38 kDa. Optimal pH and temperature for enzyme activity were 6.0 and 60 °C, respectively. The enzyme was stable up to 60 °C for 1 h and at pH 5-9 at 4 °C for 16 h. Its enzyme activity was inhibited by Hg
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Registered trials
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