Follow
International Journal of Current Microbiology and Applied Sciences (IJCMAS)
IJCMAS is now DOI (CrossRef) registered Research Journal. The DOIs are assigned to all published IJCMAS Articles.
Index Copernicus ICI Journals Master List 2018 - IJCMAS--ICV 2018: 95.39 For more details click here
National Academy of Agricultural Sciences (NAAS) : NAAS Score: *5.38 (2019) [Effective from January 1, 2019]For more details click here

Login as a Reviewer

Indexed in



National Academy of Agricultural Sciences (NAAS)
NAAS Score: *5.38 (2019)
[Effective from January 1, 2019]
For more details click here

ICV 2018: 95.39
Index Copernicus ICI Journals Master List 2017 - IJCMAS--ICV 2018: 95.39
For more details click here

See Guidelines to Authors
Current Issues

Original Research Articles

PRINT ISSN : 2319-7692
Online ISSN : 2319-7706
Issues : 12 per year
Publisher : Excellent Publishers
Email : editorijcmas@gmail.com / submit@ijcmas.com
Editor-in-chief: Dr.M.Prakash
Index Copernicus ICV 2017: 100.00
NAAS RATING 2018: 5.38

Int.J.Curr.Microbiol.App.Sci.2016.5(4): 1050-1061
DOI: http://dx.doi.org/10.20546/ijcmas.2016.504.120


Response of Free and Immobilized Uricase from Fenugreek Leaves to various treatments and Digestive Enzymes
Hamed M. El-Shora1*, AbdelAziz F. AbdelAziz2 and  Hoda M. Kondi1
1Botny Department, Faulty of Science, Mansoura University, Egypt
2Chemistry Department, Faulty of Science, Mansoura University, Egypt
*Corresponding author
Abstract:

Uricase (Urate: oxygen oxidoreductase (EC 1.7.3.3) was isolated from 15-day old Trigonella foenum-graecum L. seedlings. Kinetin, gibberellin (GA3) and benzylaminopurine induced the enzyme and kinetin was the best inducer. The polyols including mannitol, sorbitol, glycerol,erythritol and xylitol expressed appreciable thermostability for uricase at 60 ºC. Xylitol was better than trehalose as stabilizer at 60 ºC. The enzyme was then purified using 80% ammonium sulfate, DEAE-cellulose, and Sephadex G-200.  The final specific activity was 80 units mg-1 protein. The purified uricase was immobilized on alginate (entrapped)  and alginate with glutaraldehyde activity (cross-linked). The cross-linked method was better than entrapped method. The Vmax values were 15.6, 13.8 and 15.2 units mg-1 protein for the free, entrapped and cross-linked enzyme, respectively. The Km values were 0.072, 0.092 and 0.084 mM, respectively. The  optimal pH was 8.5for the free, entrapped, and cross-linked enzyme. The optimal temperature was 35 ºC , for free and entrapped but it was 45 ºC for cross-linked uricase. Uricase exhibited appreciable resistant digestion by pepsin and trypsin.


Keywords: Free and Immobilized Uricase,Fenugreek Leaves,Digestive Enzymes
Download this article as Download

How to cite this article:

Hamed M. El-Shora, AbdelAziz F. AbdelAziz and  Hoda M. Kondi. 2016. Response of Free and Immobilized Uricase from Fenugreek Leaves to Various Treatments and Digestive Enzymes.Int.J.Curr.Microbiol.App.Sci. 5(4): 1050-1061. doi: http://dx.doi.org/10.20546/ijcmas.2016.504.120