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252601

Purification, Molecular Characterization, and Anticancer Activities of L- Asparaginase extracted from Staphylococcus aureus

Article

Last updated: 01 Jan 2025

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Subjects

-

Tags

Biochemistry

Abstract

L- asparaginases catalyze the conversion of L- asparagine to L- aspartate and ammonia. The current study focus on the cloning and expression of the L-asparaginase from Staphylococcus aureus into Escherichia coli strain BL21(DE3)pLysS. L- asparaginase enzyme was purified to homogeneity by glutathione sepharose 4B column chromatography. The enzyme was purified 117.6 times and showed a final specific activity of 1680.4 IU/mg protein with a yield of 67.7%. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme showed that it was a single peptide chain with Mr 35 kDa. The enzyme was immobilized on Ca alginate beads. The immobilized enzyme retains most of its activity (78%) and reveals high stability at 4 °C. The enzymatic and structural properties of free recombinant and immobilized L- asparaginase were studied. The free enzyme showed maximum activity at pH 8.0 when incubated at 45 °C for 30 min. The immobilized enzyme displayed maximum activity at pH 8.5 after 30 minutes of incubation at 50 °C. The amino acid composition of the purified enzyme was documented. This approach offers the possibility of generating Staphylococcus aureus L- asparaginase with high efficiency that can be used to treat leukemia.

DOI

10.21608/ejchem.2022.148929.6434

Keywords

Staphylococcus aureus - L Asparaginase – Overexpression- Purification- Immobilization, Optimization

Authors

First Name

Doaa B.

Last Name

Darwish

MiddleName

-

Affiliation

Department of Biology, Faculty of Science, Tabuk University, 71491Tabuk, Saudi Arabia, Botany Department, Faculty of Science, Mansoura University,35516 Mansoura, Egypt

Email

ddarwish@ut.edu.sa

City

-

Orcid

-

First Name

Salma

Last Name

Alrdahe

MiddleName

S.

Affiliation

Department of Biology, Faculty of Science, Tabuk University, 71491Tabuk, Saudi Arabia

Email

salma_alrdahe@hotmail.com

City

-

Orcid

-

First Name

Yahya

Last Name

Al-Awthan

MiddleName

S.

Affiliation

Department of Biology, Faculty of Science, Tabuk University, 71491Tabuk, Saudi Arabia, Department of Biology, Faculty of Science, Ibb University, 70270, Ibb, Yemen

Email

alawthan@ut.edu.sa

City

-

Orcid

-

First Name

Imadeldin

Last Name

Elfaki

MiddleName

-

Affiliation

Biochemistry Department, Faculty of Science, Tabuk University, 71491Tabuk, Saudi Arabia

Email

ielfaki@ut.edu.sa

City

-

Orcid

-

First Name

Tarig

Last Name

Alnour

MiddleName

M.

Affiliation

Medical laboratory technology Department, Faculty of Applied Medical Sciences, Tabuk University, 71491Tabuk, Saudi Arabia

Email

telnour@ut.edu.sa

City

-

Orcid

0000-0001-5880-793X

First Name

Ahmed

Last Name

Darwish

MiddleName

B.

Affiliation

Zoology Department, Faculty of Science, Suez University, El Salam-1, 43533, Suez, Egypt

Email

ahmed.darwish@sci.suezuni.edu.eg

City

-

Orcid

-

First Name

Entsar

Last Name

Saad

MiddleName

A.

Affiliation

Biochemistry Division, Chemistry Department, Faculty of Science, Damietta University, New Damietta, 34511, Egypt

Email

mmm_youssef@hotmail.com

City

-

Orcid

-

First Name

Salem

Last Name

Habeb

MiddleName

A.

Affiliation

Biochemistry Department, Faculty of Science, Tabuk University, 71491Tabuk, Saudi Arabia

Email

s_habeib@yahoo.com

City

-

Orcid

-

First Name

Magdy M.

Last Name

Youssef

MiddleName

-

Affiliation

Biochemistry Division, Chemistry Department, Faculty of Science, Mansoura University, 35516 Mansoura, Egypt

Email

mmm_youssef@mans.edu.eg

City

-

Orcid

0000-0003-4205-5379

Volume

66

Article Issue

5

Related Issue

41550

Issue Date

2023-05-01

Receive Date

2022-07-04

Publish Date

2023-05-01

Page Start

245

Page End

259

Print ISSN

0449-2285

Online ISSN

2357-0245

Article File

EJCHEM_Volume 66_Issue 5_Pages 245-259.pdf

PDF . 1.6MB

Link

https://ejchem.journals.ekb.eg/article_252601.html

Detail API

https://ejchem.journals.ekb.eg/service?article_code=252601

Order

252,601

Type

Original Article

Type Code

297

Publication Type

Journal

Publication Title

Egyptian Journal of Chemistry

Publication Link

https://ejchem.journals.ekb.eg/

MainTitle

Purification, Molecular Characterization, and Anticancer Activities of L- Asparaginase extracted from Staphylococcus aureus

Details

Type

Article

Created At

30 Dec 2024