Users Online: 567
Home Print this page Email this page
Home About us Editorial board Search Browse articles Submit article Ahead of Print Instructions Subscribe Contacts Special issues Login 
ORIGINAL ARTICLE
Year : 2022  |  Volume : 11  |  Issue : 1  |  Page : 110

Expression optimizing of recombinant Oxalyl-CoA decarboxylase in Escherichia coli


1 Department of Biotechnology, School of Advanced Technologies in Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran
2 Department of Cell and Molecular Biology, Faculty of Life Sciences and Biotechnology, Shahid Beheshti University, Tehran, Iran

Correspondence Address:
Dr. Seyed Mohsen Dehnavi
Shahid Beheshti University, Daneshjoo Boulevard, Velenjak, Tehran
Iran
Login to access the Email id

Source of Support: None, Conflict of Interest: None


DOI: 10.4103/abr.abr_244_21

Rights and Permissions

Background: One of the most common diseases of the urinary tract is stones of this system, including kidney stones. About 70%–80% of kidney stones are calcium oxalate. Oxalyl-CoA decarboxylase is a single polypeptide included of 568 amino acids which play a key role in oxalate degradation. Materials and Methods: The aim of current study is high-level expression of oxalyl-CoA decarboxylase in Escherichia coli BL21 (DE3). To achieve this aim, oxalyl-CoA decarboxylase gene was cloned upon pET-30a (+) with T7 promoter. The vector containing the oxalyl-CoA decarboxylase gene was transformed into E. coli and the expression of the gene was examined on a laboratory scale and fermentor. At first, the effect of temperature, culture medium, and induction time on oxalyl-CoA decarboxylase expression at three levels was examined. Results: The obtained data showed that the highest expression was related to the terrific broth culture medium and temperature of 32°C with an inducer concentration of 1 mM. Under this situation the ultimate cells dry weight and the final oxalyl-CoA decarboxylase expression were 2.46 g/l and 36% of total protein, respectively. Then induction time was optimized in a bench bioreactor and productivity of oxalyl-CoA decarboxylase was calculated. Under optimized condition the cell density, biomass productivity and oxalyl-CoA decarboxylase concentration reached 4.02 g/l, 0.22 g/l/h, and 0.7 g/l which are one of the highest reported rates. Conclusion: This study demonstrated that high levels of oxalyl-CoA decarboxylase can be achieved by optimizing the expression conditions.


[FULL TEXT] [PDF]*
Print this article     Email this article
 Next article
 Previous article
 Table of Contents

 Similar in PUBMED
   Search Pubmed for
   Search in Google Scholar for
 Related articles
 Citation Manager
 Access Statistics
 Reader Comments
 Email Alert *
 Add to My List *
 * Requires registration (Free)
 

 Article Access Statistics
    Viewed380    
    Printed12    
    Emailed0    
    PDF Downloaded77    
    Comments [Add]    

Recommend this journal