Evidence map›Paper›PMID 41501758›Full record

ArticleBMC biotechnology2026

Statistical optimization of fermentation conditions for enhanced production of Nattokinase from Bacillus subtilis MM26.

M Maneesha, C Subathra Devi

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Article in BMC biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

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2citing papers in PubMed
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3 · Its place in the literature

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2 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

2 authors.

M ManeeshaDepartment of Biotechnology, School of Bio Sciences and Technology, Vellore Institute of Technology, Vellore, Tamil Nadu, 632014, India.
C Subathra DeviDepartment of Biotechnology, School of Bio Sciences and Technology, Vellore Institute of Technology, Vellore, Tamil Nadu, 632014, India. csubathradevi@vit.ac.in.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundNattokinase, a potent fibrinolytic serine protease enzyme has drawn significant industrial attention due to its remarkable thrombolytic activity. It is a natural alternative to conventional anticoagulant drugs because of its ability to disintegrate fibrin clots. Conventional fermentation methods frequently provide Nattokinase with poor yields, limiting production efficiency. Hence improving production strategies to enhance Nattokinase are necessary due to the growing demand for safe, efficient, and economical thrombolytic medicines worldwide. This research study aims to optimize the production parameters to enhance the Nattokinase production by Bacillus subtilis MM26, a newly isolated strain. Notably, the strain displays the unique capability to produce Nattokinase in a Menaquinone-7 (MK-7) production medium, demonstrating its adaptability.

resultsAn optimum production medium for the Nattokinase synthesis by Bacillus subtilis MM26 was identified and produced 155.1 ± 1.24 U/mL of enzyme. The significant variables influencing Nattokinase production were first identified using one factor at a time (OFAT) approach. Response surface methodology (RSM) predicted the statistically optimized conditions, resulting a yield of 3770.66 ± 0.06 U/mL. The purified enzyme was characterized using various analytical techniques including Matrix-assisted laser desorption ionization–tandem time-of-flight mass spectrometry (MALDI TOF), High Performance Liquid Chromatography (HPLC) and Fourier Transform Infrared spectroscopy (FTIR). Fibrin zymography exhibited a clear lytic band corresponding to approximately 27 kDa, confirming the fibrinolytic activity of Nattokinase.

conclusionsThe research findings highlight the ability of Bacillus subtilis MM26 for enhanced Nattokinase production. By combining OFAT and RSM, a substantial increase in the activity of enzyme was noted and the characterization validated its identity, purity and fibrinolytic efficiency. The adaptability and high productivity of the strain emphasize its suitability for economical, scalable applications in the nutraceutical or industrial applications.

Indexed as

Bacillus subtilisFermentationSubtilisinsCulture MediaVitamin K 2Culture Mediamenaquinone 7nattokinaseSubtilisinsVitamin K 2Bacillus subtilisFibrinolytic activityNattokinaseOFATOptimizationRSM

Identifiers

PMID41501758
PMCPMC12870909

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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.