The Open Biochemistry Journal




ISSN: 1874-091X ― Volume 13, 2019

Purification, Characterization and Comparison between Two New L-asparaginases from Bacillus PG03 and Bacillus PG04



Mahsa Rahimzadeh*, 1, 4, Manijeh Poodat2, Sedigheh Javadpour3, Fatemeh Izadpanah Qeshmi4, Fereshteh Shamsipour5
1 Molecular Medicine Research Center, Department of Biochemistry, Faculty of Medicine, Hormozgan University of Medical Sciences, Bandar Abbas, Iran
2 Department of Biochemistry, Faculty of Sciences, Payame Noor University of Mashhad, Mashhad, Iran
3 Molecular Medicine Research Center, Department of Microbiology, Faculty of Medicine, Hormozgan University of Medical Sciences, Bandar Abbas, Iran
4 Food and Cosmetic Health Research Center, Department of Biochemistry, Faculty of Medicine, Hormozgan University of Medical Sciences, Bandar Abbas, Iran
5 Monoclonal Antibody Research Center, Avicenna Research Institute, (ACECR), Tehran, Iran

Abstract

Background:

L-asparaginase has been used as a chemotherapeutic agent in treatment of lymphoblastic leukemia. In the present investigation, Bacillus sp. PG03 and Bacillus sp. PG04 were studied.

Methods:

L- asparaginases were produced using different culture media and were purified using ion exchange chromatography.

Results:

Maximum productivity was obtained when asparagine was used as the nitrogen source at pH 7 and 48 h after cultivation. New intracellular L-asparaginases showed an apparent molecular weight of 25 kDa and 30 kDa by SDS-PAGE respectively. These enzymes were active in a wide pH range (3-9) with maximum activity at pH 6 for Bacillus PG03 and pH 7 for Bacillus PG04 L-asparaginase. Bacillus PG03 enzyme was optimally active at 37 ˚C and Bacillus PG04 maximum activity was observed at 40˚C. Kinetic parameters km and Vmax of both enzymes were studied using L-asparagine as the substrate. Thermal inactivation studies of Bacillus PG03 and Bacillus PG04 L-asparaginase exhibited t1/2 of 69.3 min and 34.6 min in 37 ˚C respectively. Also T50 and ∆G of inactivation were measured for both enzymes.

Conclusion:

The results revealed that both enzymes had appropriate characteristics and thus could be a potential candidate for medical applications.

Keywords: Bacillus PG03, Bacillus PG04, L-asparaginase, Purification, Thermostability.


Article Information


Identifiers and Pagination:

Year: 2016
Volume: 10
First Page: 35
Last Page: 45
Publisher Id: TOBIOCJ-10-35
DOI: 10.2174/1874091X01610010035

Article History:

Received Date: 7/02/2016
Revision Received Date: 25/08/2016
Acceptance Date: 22/09/2016
Electronic publication date: 04/11/2016
Collection year: 2016

Article Metrics:

CrossRef Citations:
0

Total Statistics:

Full-Text HTML Views: 2119
Abstract HTML Views: 743
PDF Downloads: 306
ePub Downloads: 169
Total Views/Downloads: 3337

Unique Statistics:

Full-Text HTML Views: 855
Abstract HTML Views: 465
PDF Downloads: 226
ePub Downloads: 123
Total Views/Downloads: 1669
Geographical View

© Rahimzadeh et al.; Licensee Bentham Open

open-access license: This is an open access article licensed under the terms of the Creative Commons Attribution-Non-Commercial 4.0 International Public License (CC BY-NC 4.0) (https://creativecommons.org/licenses/by-nc/4.0/legalcode), which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.


* Address correspondence to this author at the Department of Biochemistry, Faculty of Medicine, Hormozgan University of Medical Sciences, Emam Hossein Boulevard, P.O. Box: 7919693116, Bandar Abbas, Iran; Tel: +98-761-6688024; Fax: +98-761-6668478; E-mail: mahsa_rahimzadeh@yahoo.com


Endorsements



"We have always had a fruitful cooperation and long-term experience of publishing with Bentham Open."

"A number of our original papers have appeared in its different journals, as the Bentham Open Publishers provides sufficient research in the field of science and technologies (belonging to the pharmaceutical, biotechnology, biomedical industries etc). The staff of the Bentham Open always treat our papers very seriously and gently during the rutile paper reviewing process, so far we always felt their kindness and highly cooperative support. Today, Bentham Open is providing a great support to science and research, giving opportunities of high standard publishing as well as promoting and enhancing selected papers around the world through communication and exchange of global scientific education."


Kholmirzo T. Kholmurodov
Leading Scientist
FLNP (Frank Laboratory of Neutron Physics) JINR (Joint Institute of Nuclear Research) Moscow region, Russia


Browse Contents



Webmaster Contact: info@benthamopen.net
Copyright © 2019 Bentham Open