Normal view MARC view ISBD view

Purification and characterization of extracellular Penicillium brevicompactum uricase [electronic resource].

By:

El-Bessoumy, Ashraf A

Language: English Summary language: Arabic Description: P. 161-168Other title:

تنقية وتوصيف انزيم اليوريكاز المتحمل للحرارة من فطر البينيسليم بريفيكومباكتم [Added title page title]

Uniform titles:

Zagazig veterinary journal, 2009 v. 37 (2) [electronic resource].

Subject(s):

Online resources:

Full Text Article

In: Zagazig Veterinary Journal 2009.v.37(2)Summary: The uricase was purified to homogeneity from Penicillium brevicompactum grown on solid state fermentation. Different purification steps including ammonium sulfate fractionation followed by separation on DEAE-Spheadex A50 and Sephadex-G75 column were applied to the crude culture filtrate to obtain a pure enzyme. The enzyme was purified 64.59 fold and shoed a final specific activity of 3920 U/mg protein with 51.7 % yield. SDS-PAGE of the purified enzyme revealed it was one peptide chain with molecular weight of 43 kDa. Line Weaver-Burk analysis showed a km value of 0.5 mM and Vmax of 909 Iu. Maximum enzyme activity was found at pH 9 and 30°C. The purified enzyme showed maximum stability over a wide rang of pH between 6-10and up to temperature of 70°C. The enzyme activity was stimulated greatly in presence Fe, Na, Ca, and Cu ions and inhibited greatly by addition of EDTA and KCN. The pure enzyme proved to be rich in methionine, glutamic acid and glycine.

Average rating: 0.0 (0 votes)

No physical items for this record

Includes references.

The uricase was purified to homogeneity from Penicillium brevicompactum grown on solid state fermentation. Different purification steps including ammonium sulfate fractionation followed by separation on DEAE-Spheadex A50 and Sephadex-G75 column were applied to the crude culture filtrate to obtain a pure enzyme. The enzyme was purified 64.59 fold and shoed a final specific activity of 3920 U/mg protein with 51.7 % yield. SDS-PAGE of the purified enzyme revealed it was one peptide chain with molecular weight of 43 kDa. Line Weaver-Burk analysis showed a km value of 0.5 mM and Vmax of 909 Iu. Maximum enzyme activity was found at pH 9 and 30°C. The purified enzyme showed maximum stability over a wide rang of pH between 6-10and up to temperature of 70°C. The enzyme activity was stimulated greatly in presence Fe, Na, Ca, and Cu ions and inhibited greatly by addition of EDTA and KCN. The pure enzyme proved to be rich in methionine, glutamic acid and glycine.

Summary in Arabic.

There are no comments on this title.

to post a comment.