Partial purification and some properties of a phospholipase C from Pseudomonas sp. strain KS3.2.
نویسندگان
چکیده
An extracellular phospholipase C was partially purified from Pseudomonas sp. strain KS3.2. The enzyme was composed of an approximately 18-kDa peptide. Maximal enzyme activity was found at pH 7.2 and 50 degrees C. The enzyme retained activity between pH 8 and 9, and 50% activity at about 52 degrees C for 30 min. The enzyme sample showed the highest activity on phosphatidylcholine and low activity toward other phospholipids.
منابع مشابه
Purification and Characterization of a Thermostable Neutrophilic Metalloprotease from Pseudomonas sp. DR89
A novel neutrophilic metalloprotease was isolated from Pseudomonas sp. DR89 isolate which was identified ina mineral spring in Iran. The enzyme was purified from the isolate to 21-folds in a three-step procedure involving ammonium sulfate precipitation, Q-Sepharose ionic exchange and Sephadex G-100 gel filtrationchromatography. Resuts showed that the enzyme was active at high temper...
متن کاملPurification and characterization of an acidic, thermophilic phytase from a newly isolated Geobacillus stearothermophilus strain DM12
Microbial phytases were applied mainly to animal and human foodstuffs in order to improvemineral bioavailability and food processing. In addition, phytases have potentialbiotechnological application in various other fields, such as environmental protection,aquaculture and agriculture. Bacillus sp. DM12, an isolate from a hot spring, produces phytase,which catalyzes the hydrolysis of phytic acid...
متن کاملبررسی رابطه ژن‌های فسفولیپاز C با پاتوژنیسیته مایکوباکتریوم توبرکلوزیس سویه بیجینگ وسویه غیربیجینگ
Abstract Background: The Beijing strain of Mycobacterium tuberculosis is responsible for more than 25% of cases of Tuberculosis in the world, it has a high transmission potential and there is a significant correlation between Beijing strain and multidrug resistance. In this study we compared the presence of Phospholipase C genes in Beijing and Nonbeijing strains of Mycobacterium tuberculosis...
متن کاملPurification and Characterization of Alginate Lyase from Mucoid Pseudomonas aeruginosa Strain 214
Pseudomonas aeruginosa is an opportunistic pathogen that causes a variety of infections in compromised patients. The ability of Pseudomonas aeruginosa to produce chronic infection is based in part on its ability to biosynthesis of biofilm, and alginate is the major polysaccharide in the synthesized biofilm. So alginate degradation is very essential in the dispersion of Pseudomonas aeruginosa bi...
متن کاملPurification and Characterization of a Novel Thermostable and Acid Stable α-Amylase from Bacillus Sp. Iranian S1
This study reports the purification and biochemical characterization of thermostable and acidic-pH-stable α-amylase from Bacillus sp. Iranian S1 isolated from the desert soil (Gandom-e-Beryan in Lut desert, Iran). Amylase production was found to be growth associated. Maximum enzyme production was in exponential phase with activity 2.93 U ml-1 at 50°C and pH 5. The enzyme was purified by isoprop...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Bioscience, biotechnology, and biochemistry
دوره 70 2 شماره
صفحات -
تاریخ انتشار 2006