Purification, Characterization and Molecular Studies on Oxalate Decarboxylase from B. cepacia inhabits Egyptian soil
Abou Shady, H., Kilany, M., Genedi, Q., Farouk, W. (2013). Purification, Characterization and Molecular Studies on Oxalate Decarboxylase from B. cepacia inhabits Egyptian soil. EKB Journal Management System, 5(2), 77-86. doi: 10.21608/eajbsc.2013.16097
Hala Abou Shady; Mona Kilany; Qadria Genedi; Wafaa Farouk. "Purification, Characterization and Molecular Studies on Oxalate Decarboxylase from B. cepacia inhabits Egyptian soil". EKB Journal Management System, 5, 2, 2013, 77-86. doi: 10.21608/eajbsc.2013.16097
Abou Shady, H., Kilany, M., Genedi, Q., Farouk, W. (2013). 'Purification, Characterization and Molecular Studies on Oxalate Decarboxylase from B. cepacia inhabits Egyptian soil', EKB Journal Management System, 5(2), pp. 77-86. doi: 10.21608/eajbsc.2013.16097
Abou Shady, H., Kilany, M., Genedi, Q., Farouk, W. Purification, Characterization and Molecular Studies on Oxalate Decarboxylase from B. cepacia inhabits Egyptian soil. EKB Journal Management System, 2013; 5(2): 77-86. doi: 10.21608/eajbsc.2013.16097

Purification, Characterization and Molecular Studies on Oxalate Decarboxylase from B. cepacia inhabits Egyptian soil

Egyptian Academic Journal of Biological Sciences. C, Physiology and Molecular Biology
Article 8, Volume 5, Issue 2, December 2013, Page 77-86  XML PDF (186.94 K)
Document Type: Original Article
DOI: 10.21608/eajbsc.2013.16097
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Authors
Hala Abou Shady1; Mona Kilany2; Qadria Genedi2; Wafaa Farouk1
1Microbiology Dept., Faculty of Science, Ain Shams University, Cairo, Egypt
2Microbiology Dept., National Organization for Drug Control and Research (NODCAR), Cairo, Egypt
Abstract
Oxalate decarboxylase (OXDC) is an intracellular enzyme that decomposes toxic oxalate into formate and CO2. So, it is used for medical diagnosis of oxalate and decreasing the oxalate level. OXDC enzyme was purified from B. cepacia, characterized and subjected to amino acid analysis. Genomic and plasmid DNA from B. cepacia were purified. PCR products of OXDC gene was subjected to DNA sequence analysis. OXDC was purified 18.05 folds to near homogeneity with a specific activity of 4.496 U/ μg protein and showed pure single band with molecular weight 30 kDa. OXDC showed an optimal activity at pH 6, 35C° using Zn+2 and Mn+2 as a catalyst. The most abundant amino acid is alanine and the less frequent amino acid is cysteine. Comparing the genomic and plasmid DNA showed that both have the same size. Similarity search results showed that the obtained sequence can detect OXDC gene in many B. cepacia genomes.
This work is supported byNational Organization for Drug Control and Research (NODCAR), Cairo, Egypt
Keywords
Oxalate decarboxylase; plasmid; genomic DNA; B. cepacia
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