Optimization and partial purification of extracellular phytase from Pseudomonas aeruginosa p6

نویسنده

  • B. Sasirekha
چکیده

Fifty isolates capable of producing phytase were isolated from various soil samples. Out of fifty isolates five isolates showed maximum phytase activity. P6 isolate was selected for further study P6 isolate was biochemically characterized as Pseudomonas spp. The culture conditions were optimized for maximum enzyme production. The best carbon and nitrogen sources for maximum phytase production were 1% glucose and 0.5% yeast extract respectively. The enzyme was stable between the pH 4 to 10 but the optimal pH was found to be 6. The enzyme was also stable between temperature ranges 30 C to 50C but best temperature for enzyme activity was found to be 37 C. Maximum phytase activity was 98.76 U/ml after 24 hrs of incubation under optimal conditions. The specific activity of the crude enzyme was 31.86Umg protein and this was increased to 70.77Umgprotein by (NH4)2SO4 precipitation.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

One-step purification and characterization of alginate lyase from a clinical Pseudomonas aeruginosa with destructive activity on bacterial biofilm

Objective(s): Pseudomonas aeruginosais a Gram-negative and aerobic rod bacterium that displays mucoid and non-mucoid phenotype. Mucoid strains secrete alginate, which is the main agent of biofilms in chronic P. aeruginosa infections, show high resistance to antibiotics; consequently, the biological disruption of mucoid P. aeruginosa biofilms is an attractive area of study for researchers. Algin...

متن کامل

Optimization of Lipase Immobilization

Pseudomonas aeruginosa BBRC-10036 was used for lipase production. The organism secreted the enzyme extracellulary. In order to purify the enzyme, precipitation was done first, and then this lipase has been purified by Ion exchange Chromatography leading to 2.3-fold purification and 11.47% recovery. Lipase from P.aeruginosa was entrapped into Ca-alginate gel beads and effect of independent varia...

متن کامل

Partial Purification of the Extracellular Hemolysin of Pseudomonas Aeruginosa.

Berk, Richard S. (Wayne State University, College of Medicine, Detroit, Mich.). Partial purification of the extracellular hemolysin of Pseudomonas aeruginosa. J. Bacteriol. 88:559-565. 1964.-Through a series of chemical fractionation steps, the extracellular hemolysin of Pseudomonas aeruginosa was purified 126-fold with a recovery of 49%. Hemolytic activity of crude preparations was irreversibl...

متن کامل

Expression, purification and preliminary crystallographic analysis of Pseudomonas aeruginosa RocR protein.

Pseudomonas aeruginosa RocR, an EAL-domain protein which regulates the expression of virulence genes and biofilm formation, has been cloned and expressed in Escherichia coli and purified. Here, the crystallization and preliminary diffraction analysis of RocR are reported. The X-ray diffraction data were processed to a resolution of 2.50 A. The crystals belonged to space group P6(1)22 or P6(5)22...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2012