ArticleBMC biotechnology2021
Heterologous expression of nattokinase from B. subtilis natto using Pichia pastoris GS115 and assessment of its thrombolytic activity.
Article in BMC biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Transcriptome study ofMicrobiology spectrum · 2026Article
- Engineered Bacillus subtilis for high-yield nattokinase production and therapeutic potential in obesity management.Journal of animal science and biotechnology · 2026Article
- Enhanced nattokinase production by optimized fermentation conditions of douchi-derived Bacillus subtilis natto NK11 and evaluation of its thrombolytic activity.Antonie van Leeuwenhoek · 2025Article
- Transient expression of full-length and mature nattokinase in Nicotiana benthamiana reveals early necrosis from full-length form and functional activity of the mature enzyme.Frontiers in plant science · 2025Article
- Nattokinase Attenuated Excitatory Amino Acids and Cytokines Release and Restored Cerebral Blood Flow in a Thrombolytic Focal Cerebral Ischemic Rat Model.Central nervous system agents in medicinal chemistry · 2025Article
- Heterologous Expression of KetoreductaseMolecules (Basel, Switzerland) · 2024Article
- Review
- Modification of the active centre of nattokinase to enhance its thermostability using a strategy based on molecular dynamics simulation, steered dynamics simulation, and conservative prediction.Frontiers in nutrition · 2024Article
- Research progress on the fibrinolytic enzymes produced from traditional fermented foods.Food science & nutrition · 2023Review
- Combined Computer-Aided Predictors to Improve the Thermostability of Nattokinase.Foods (Basel, Switzerland) · 2023Article
- Heterologous Expression of Extracellular Proteinase pAsPs ofInternational journal of molecular sciences · 2022Article
- The potential role of ischaemia-reperfusion injury in chronic, relapsing diseases such as rheumatoid arthritis, Long COVID, and ME/CFS: evidence, mechanisms, and therapeutic implications.The Biochemical journal · 2022Review
- Characterization of a Nattokinase from the Newly Isolated Bile Salt-ResistantFoods (Basel, Switzerland) · 2022Article
- Heterologous Expression of Xylanase xAor from Aspergillus oryzae in Komagataella phaffii T07International journal of molecular sciences · 2022Article
- Biotechnology, Bioengineering and Applications ofBiomolecules · 2022Review
- Recent Advances in Nattokinase-Enriched Fermented Soybean Foods: A Review.Foods (Basel, Switzerland) · 2022Review
- Oral Administration of Nanopeptide CMCS-20H Conspicuously Boosts Immunity and Precautionary Effect Against Bacterial Infection in Fish.Frontiers in immunology · 2021Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundNattokinase is a fibrinolytic enzyme that has huge market value as a nutritional supplement for health promotion. In order to increase nattokinase yields, fermentation conditions, strains, cultivation media, and feeding strategies have been optimized. Nattokinase has been expressed using several heterologous expression systems. Pichia pastoris heterologous expression system was the alternative.
resultsThis report aimed to express high levels of nattokinase from B. subtilis natto (NK-Bs) using a Pichia pastoris heterologous expression system and assess its fibrinolytic activity in vivo. Multicopy expression strains bearing 1-7 copies of the aprN gene were constructed. The expression level of the target protein reached a maximum at five copies of the target gene. However, multicopy expression strains were not stable in shake-flask or high-density fermentation, causing significant differences in the yield of the target protein among batches. Therefore, P. pastoris bearing a single copy of aprN was used in shake-flask and high-density fermentation. Target protein yield was 320 mg/L in shake-flask fermentation and approximately 9.5 g/L in high-density fermentation. The recombinant nattokinase showed high thermo- and pH-stability. The present study also demonstrated that recombinant NK-Bs had obvious thrombolytic activity.
conclusionsThis study suggests that the P. pastoris expression system is an ideal platform for the large-scale, low-cost preparation of nattokinase.
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