Skip to main content
Log in

Isolation, identification, and optimization of the fibrinolytic protease-producing strains

  • Original Paper
  • Published:
Archives of Microbiology Aims and scope Submit manuscript

Abstract

Cardiovascular complications due to thrombosis have become one of the main causes of death worldwide. The high cost and undesirable side effects of existing thrombolytic agents have led researchers to isolate potential strains that produce fibrinolytic enzymes for therapeutic applications. Fibrinolytic enzymes, especially of microbial origin, are recognized as potential therapeutic candidates for thrombosis. In this study, isolation, identification, and optimization of fibrinolytic protease enzyme-producing strains were performed using fermentative protein sources. Fibrinolytic protease-producing strains were selected by analyzing the isolated strains on skim milk agar medium. The selected strains were examined on blood agar and fibrin plate medium, and the ones showing high enzymatic activity were determined. The strain determined to have the highest activity was identified as Acinetobacter johnsonii TR01 by 16S rRNA analysis. The maximum fibrinolytic protease production of the strain occurred at 60 °C and pH 7.0. Under different medium conditions used for enzyme production, fructose was found to be the best carbon source, while yeast extract and peptone were the best nitrogen sources. It was observed that CaCl2, KH2PO4, and MgSO4 components had a negative effect, while MnCl2 and ZnC4H6O4 components had a positive effect on enzyme production. The medium composition for maximum enzyme activity (8.30 IU/ml) determined by Response Surface Methodology was 14.22 g/L fructose, 11.190 g/L yeast extract, 14.22 g/L peptone, 0.5 g/L MnCl2, and 0.5 g/L ZnC4H6O4.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7
Fig. 8
Fig. 9
Fig. 10
Fig. 11
Fig. 12

Similar content being viewed by others

Availability of data and materials

The datasets generated during and/or analyzed during the current study are available from the corresponding author on reasonable request.

References

Download references

Funding

Not funding.

Author information

Authors and Affiliations

Authors

Contributions

All the authors contributed to the study conception and design. Material preparation, data collection, and analysis were performed by BU, MŞT, and AG. The first draft of the manuscript was written by BU and all the authors commented on previous versions of the manuscript. All the authors read and approved the final manuscript.

Corresponding author

Correspondence to Abdulkadir Gül.

Ethics declarations

Conflict of interest

The authors have no relevant financial or non-financial interests to disclose.

Ethical approval

This article does not contain any studies with animals or human participants.

Consent to participate

The authors agreed to participate in this work.

Consent for publication

The authors agreed to publish this work.

Additional information

Communicated by Pankaj Bhatt.

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Umay, B., Gül, A. & Tanyıldızı, M.Ş. Isolation, identification, and optimization of the fibrinolytic protease-producing strains. Arch Microbiol 205, 135 (2023). https://doi.org/10.1007/s00203-023-03486-z

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • DOI: https://doi.org/10.1007/s00203-023-03486-z

Keywords

Navigation