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Paper Information

Journal:   IRANIAN JOURNAL OF PUBLIC HEALTH   AUGUST 2014 , Volume 43 , Number SUPPLEMENT 2; Page(s) 44 To 44.
 
Paper: 

PURIFICATION AND DETERMINATION OF OPTIMUM PH AND TEMPERATURE OF INTRACELLULAR L-ASPARAGINASE FROM BACILLUS SP.PG-02

 
 
Author(s):  RAHIMZADEH MAHSA*
 
* DEPARTMENT OF BIOCHEMISTRY, FACULTY OF MEDICINE AND MOLECULAR MEDICINE RESEARCH CENTER, HORMOZGAN UNIVERSITY OF MEDICAL SCIENCE, BANDAR ABBAS, IRAN
 
Abstract: 

Background: Bacterial L-asparaginases are amid hydrolases that catalyze the conversion of L-asparagine to L-aspartate and ammonia. The enzymes isolated from E. coli and Erwinia carotovora are now being used in the treatment of acute lymphoblastic leukemia. However, prolonged administration of L-asparaginase causes an anaphylactic shock or neutralization of the drug effect. Therefore there is a continuing need to screen newer organisms in order to obtain strains capable of producing new and high yield of L-asparaginase. In the present study a novel strain, Bacillus sp.PG-02 was explored for the production of intra-cellular L-asparaginase.
Methods: Bacillus sp.PG-02 was grown in a modified M9 medium and incubated in a rotary shaking incubator. After 24 h of inoculation, the cells were removed by centrifugation. Sonication of the cells was carried out to release the intracellular L-asparaginase and DEAE-Cellulose Ion exchange chromatography with discontinuous gradient of NaCl was used for purification of enzyme. The optimum pH and temperature for L-asparaginase activity were determined. The molecular weight of the purified enzyme was estimated by SDS-PAGE.
Results: The bacterial strain, Bacillus PG-02 was isolated from the Persian Gulf sediments and screened for the ability of L- asparaginase production. The intracellular enzyme was then purified through DEAE column. The enzyme was eluted in 0.2 M NaCl. SDS-PAGE analysis showed that the enzyme was purified and its molecular weight was approximately 35 kDa. Enzyme demonstrated the maximum activity at pH 7.5. The optimum temperature of the activity of the enzyme was found to be 40oC.
Conclusion: The purified L-asparaginase produced by Bacillus sp.PG-02 showed a good activity near the physiological condition. Thus, it is a potential candidate for medical applications.

 
Keyword(s): L-ASPARAGINASE, BACILLUS, PURIFICATION, ACTIVITY
 
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