Document Details

Document Type : Thesis 
Document Title :
Genetic improvement and Molecular characterization of bacterial isolate producing uricase enzyme
التحسین الوراثي والتوصیف الجزیئي لعزلة بكتیریة منتجة لإنزیم الیوریكیز
 
Document Language : English 
Abstract : Urate oxidase (EC 1.7.3.3) or uricaseis a tetrameric enzyme of therapeutic interest implicated in the catalyzed degradation of uric acid, (a final product of purine catabolism, to allantoin, which is more soluble and more easily to be excreted than the starting compound). Twenty five isolates of microorganisms were screened for uricase productionwith medium containing uric acid as the only carbon source. All isolates were obtained from samples of soil and water, collected from different places of Jeddah, Saudi Arabia. The degradation of uric acid in bacterial isolates with different taxonomical properties was investigated. The amount of uricase was determined by spectrophotometry. Five isolates out of 25 (20%) of the tested isolates produced uricase. The highest uricase producer was the isolate (SK3) thus; it was selected for more detail studies. Based on its morphological, biochemical and physiological characteristics, as well as 16srDNA sequence and phylogenetic analysis, this isolate was identified as Bacillus cereusSK3. The effects of different factors on the enzyme production were studied. It was showed that glucose/tryptone broth medium was the most favorable one, the optimum temperature was at 30°C, and incubation period required for maximum production was 3 day with aeration level at 150 rpm and pH 8.0. Different carbon sources and nitrogen sources were used for bacterial growth and uricase production. Glucose proved to be the best carbon source, peptone was found to be the best nitrogen source. Moreover, uricase production was enhanced using mutation. The obtainedmutant grows well and produces higher uricase, 6times more compared to the original isolate 
Supervisor : Sanaa Tork 
Thesis Type : Master Thesis 
Publishing Year : 1434 AH
2012 AD
 
Number Of Pages : 111 
Co-Supervisor : Magda Mohammad Aly 
Added Date : Monday, December 15, 2014 

Researchers

Researcher Name (Arabic)Researcher Name (English)Researcher TypeDr GradeEmail
صفا قطب الفتنيAl-Fattani, Safa QutubInvestigatorMaster 

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