Study of the stability of uricase from Aspergillus flavus and its stabilization by Glucose

Q: How can I download an article?

To download an article from SID, first log in to the site, search for the article title, and click on the 'Download Article' option.

Q: How can I download an ISI article?

To download an ISI article on SID, enter the keyword or article title in the search bar, view the relevant results, click on the desired article, and select the 'Download Article' option.

Q: How can I access the SID database?

To access the SID database, visit SID.ir, create an account, and log in to access scientific resources.

Q: Is downloading articles from SID free?

Some articles on SID are available for free, while others require payment. Details are specified on the article's page.

mirzainiya somayeh; Pazhang Mohamad; IMANI MAHDI

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Journal Paper

Paper Information

Journal: JOURNAL OF BIOTECHNOLOGY Year:2017 | Volume:8 | Issue:1 Page(s): 55-64

Download Full-Text

Persian Verion

View:

869

Download:

Cites:

Information Journal Paper

Title

Study of the stability of uricase from Aspergillus flavus and its stabilization by Glucose

Author(s)

mirzainiya somayeh | Pazhang Mohamad | IMANI MAHDI | Issue Writer Certificate

Keywords

Uric acidQ1

UricaseQ1

StabilizationQ1

AdditivesQ2

glucoseQ1

Abstract

Uricase or urate oxidase is an enzyme that converts Uric acid (with low solubility) to 5-hydroxyisourate and finally to allantoin. The possibility of developing some diseases like gout and kidney stones will be increased in high levels of Uric acid. Thus, Uricase can be used as drug enzyme to reduce Uric acid levels in the blood. The low stability of proteins (such as drug enzymes) is a challenge in the use of them. There are several approaches such as use of Additives for protein Stabilization. In this study, E. Coli BL21 (DE3) was transformed by pET28a (+) vector carrying Aspergillus flavus Uricase gene. The recombinant protein was expressed and then purified by a Ni-NTA agarose chromatography column. After purification, the thermal stability of the purified enzyme was evaluated and then it stabilized by Additives. The results showed that enzyme is active and purified very well. Thermal stability results indicated that Uricase maintains its stability up to 20° C and then loses its stability. The half-life of enzyme was 30minutes at 40 ° . The results of enzyme Stabilization by 20% (v/w) concentration of glucose and sorbitol as well as by 20 % (v/v) of glycerol showed that glucose had the most Stabilization effect on the Uricase among the Additives. The stability (half life) of enzyme was increased more than two times in the presence of glucose. Finally, we conclude that Additives like glucose which increase surface tension have the most Stabilization effect on the Uricase enzyme stability.

Cites

No record.

References

No record.

Cite

APA: Copy

mirzainiya, somayeh, Pazhang, Mohamad, & IMANI, MAHDI. (2017). Study of the stability of uricase from Aspergillus flavus and its stabilization by Glucose. JOURNAL OF BIOTECHNOLOGY, 8(1 ), 55-64. SID. https://sid.ir/paper/231330/en

Vancouver: Copy

mirzainiya somayeh, Pazhang Mohamad, IMANI MAHDI. Study of the stability of uricase from Aspergillus flavus and its stabilization by Glucose. JOURNAL OF BIOTECHNOLOGY[Internet]. 2017;8(1 ):55-64. Available from: https://sid.ir/paper/231330/en

IEEE: Copy

somayeh mirzainiya, Mohamad Pazhang, and MAHDI IMANI, “Study of the stability of uricase from Aspergillus flavus and its stabilization by Glucose,” JOURNAL OF BIOTECHNOLOGY, vol. 8, no. 1 , pp. 55–64, 2017, [Online]. Available: https://sid.ir/paper/231330/en

Related Journal Papers