ArticleScientific reports2016
A new strategy to express the extracellular α-amylase from Pyrococcus furiosus in Bacillus amyloliquefaciens.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 34 citations in OpenAlex.
- Bacillus and Streptomyces spp. as hosts for production of industrially relevant enzymes.Applied microbiology and biotechnology · 2024Review
- Evaluation of the Physical Stability of Starch-Based Hydrogels Produced by High-Pressure Processing (HPP).Gels (Basel, Switzerland) · 2022Article
- Multiple Modular Engineering ofFrontiers in bioengineering and biotechnology · 2022Article
- Enhanced Production of SolubleJournal of microbiology and biotechnology · 2021Article
- Development of Bacillus amyloliquefaciens as a high-level recombinant protein expression system.Journal of industrial microbiology & biotechnology · 2019Article
- Biotechnology of extremely thermophilic archaea.FEMS microbiology reviews · 2018Review
- An Insight Into Ameliorating Production, Catalytic Efficiency, Thermostability and Starch Saccharification of Acid-Stable α-Amylases From Acidophiles.Frontiers in bioengineering and biotechnology · 2018Review
- Bottleneck in secretion of α-amylase in Bacillus subtilis.Microbial cell factories · 2017Review
- A hyper-thermostable α-amylase from Pyrococcus furiosus accumulates in Nicotiana tabacum as functional aggregates.BMC biotechnology · 2017Article
- A novel strategy to improve protein secretion via overexpression of the SppA signal peptide peptidase in Bacillus licheniformis.Microbial cell factories · 2017Article
- Biotechnological Processes in Microbial Amylase Production.BioMed research international · 2017Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Extracellular α-amylase from Pyrococcus furiosus (PFA) shows great starch-processing potential for industrial application due to its thermostability, long half-life and optimal activity at low pH; however, it is difficult to produce in large quantities. In contrast, α-amylase from Bacillus amyloliquefaciens (BAA) can be produced in larger quantities, but shows lower stability at high temperatures and low pH. Here, we describe a BAA protein expression pattern-mimicking strategy to express PFA in B. amyloliquefaciens using the expression and secretion elements of BAA, including the codon usage bias and mRNA structure of gene, promoter, signal peptide, host and cultivation conditions. This design was assessed to be successful by comparing the various genes (mpfa and opfa), promoters (PamyA and P43), and strains (F30, F31, F32 and F30-∆amyA). The final production of PFA yielded 2714 U/mL, about 3000- and 14-fold that reportedly produced in B. subtilis or E. coli, respectively. The recombinant PFA was optimally active at ~100 °C and pH 5 and did not require Ca(2+) for activity or thermostability, and >80% of the enzyme activity was retained after treatment at 100 °C for 4 h.
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