419088

Optimized Expression and Activity Assessment of Bacterial Staphylokinase in E. coli BL21(DE3)

Article

Last updated: 29 Mar 2025

Subjects

-

Tags

Genetics

Abstract

Background: The application of recombinant proteins is rare following the high production costs of expressing proteins with expensive inducers, such as isopropyl-β-D-1-thiogalactopyranoside (IPTG). Staphylokinase (SAK), a fibrinolytic enzyme, is a small bacterial thrombolytic agent that specifically clots and converts plasminogens to plasmins and lysis fibrin clots. Objective: The primary aim of the present investigation is increasing the yield and lower the cost of staphylokinase production using Escherichia coli BL21 (DE3). Methodology: The influence of target protein in expression host by different culture medium, culture density, and IPTG concentration on the expression of SAK protein was explored. Results: The results indicated that only the culture density and concentration of IPTG were significant. This study achieved cost reduction by decreasing the IPTG inducer concentration (1.0 and 0.5mM), which acted as the inducer. The production rate was also maintained or increased in low culture density. Conclusion: Suitable production conditions, particularly diminished inducer concentration, effectively reduced upstream production costs and yielded high sak gene expression protein as an active form.

DOI

10.21608/ejmm.2025.368878.1524

Keywords

Staphylokinase, E. coli, protein expression, Culture density, IPTG

Authors

First Name

Harith

Last Name

Buniya

MiddleName

K.

Affiliation

Department of Biology, College of Education for Pure Science, University Of Anbar, Ramadi 31001, Al-Anbar, Iraq

Email

hkbuniya@uoanbar.edu.iq

City

Ramadi

Orcid

0000-0002-5232-618X

First Name

Omer

Last Name

Salahdin

MiddleName

D.

Affiliation

Department of Biology, College of Education for Pure Science, University Of Anbar, Ramadi 31001, Al-Anbar, Iraq

Email

omer9922ff@uoanbar.edu.iq

City

Ramadi

Orcid

-

First Name

Abdulsalam

Last Name

Mohammed

MiddleName

N.

Affiliation

Department of Medical Laboratory Techniques, College of Health and Technology, University of Al-Maarif, Ramadi 31001, Al-Anbar, Iraq

Email

abdulsalam.najim@uoa.edu.iq

City

Ramadi

Orcid

-

Volume

34

Article Issue

3

Related Issue

53640

Issue Date

2025-07-01

Receive Date

2025-03-17

Publish Date

2025-07-01

Print ISSN

1110-2179

Online ISSN

2537-0979

Link

https://ejmm.journals.ekb.eg/article_419088.html

Detail API

http://journals.ekb.eg?_action=service&article_code=419088

Order

419,088

Type

New and original researches in the field of Microbiology.

Type Code

2,038

Publication Type

Journal

Publication Title

Egyptian Journal of Medical Microbiology

Publication Link

https://ejmm.journals.ekb.eg/

MainTitle

Optimized Expression and Activity Assessment of Bacterial Staphylokinase in E. coli BL21(DE3)

Details

Type

Article

Created At

29 Mar 2025