Thermostable Alkaline Phytase from Alcaligenes sp. in Improving Bioavailability of Phosphorus in Animal Feed: In Vitro Analysis

نویسندگان

  • Ponnuswamy Vijayaraghavan
  • R. Raja Primiya
  • Samuel Gnana Prakash Vincent
چکیده

A bacterial isolate, Alcaligenes sp. secreting phytase (EC 3.1.3.8), was isolated and characterized. The optimum conditions for the production of phytase included a fermentation period of 96 h, pH 8.0, and the addition of 1% (w/v) maltose and 1% (w/v) beef extract to the culture medium. This enzyme was purified to homogeneity and had an apparent molecular mass of 41 kDa. The optimum pH range and temperature for the activity of phytase were found to be 7.0-8.0 and 60°C, respectively. This enzyme was strongly inhibited by 0.005 M of Mn(2+), Mg(2+), and Zn(2+). In vitro studies revealed that the phytase from Alcaligenes sp. released inorganic phosphate from plant phytates. Phytase released 1930 ± 28, 1740 ± 13, 1050 ± 31, 845 ± 7, 1935 ± 32, and 1655 ± 21 mg inorganic phosphate/kg plant phytates, namely, chick pea, corn, green pea, groundnut, pearl pea, and chick feed, respectively.

برای دانلود 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

Bioinformatics Analysis of Upstream Region and Protein Structure of Fungal Phytase Gene

Phytase increases the bioavailability of phytate phosphorus in seed-based animal feeds and reduces the phosphorus pollution of animal waste. Since most animal feeds for pellets are heated up to 65-80 °C, the production of a thermostable structure for phytase can be useful. In this study, we sought to perform bioinformatics analysis of the upstream region and protein structure of fungal phytase ...

متن کامل

The influence of enzymatic pre-treatment of corn or soybean meal on their phytate content under different in vitro conditions

BACKGROUND: Phosphorous is one of the expensive nutrients in poultry feed. Therefore, improving the bioavailability of this nutrient in feed ingredients could be effective for lowering the cost of feed. OBJECTIVE: This study was performed to evaluate the effect of pre-treatment of feed ingredients by commercial enzymes and different levels of pH on releasing of phosphorus from phytate under in ...

متن کامل

Phytase activity in Cryptococcus laurentii ABO 510.

Ten Cryptococcus strains were screened for phytase activity, of which the Cryptococcus laurentii ABO 510 strain showed the highest level of activity. The cell wall-associated enzyme displayed temperature and pH optima of 62 degrees C and 5.0, respectively. The enzyme was thermostable at 70 degrees C, with a loss of 40% of its original activity after 3 h. The enzyme was active on a broad range o...

متن کامل

Comparative Analysis of Peripheral Alkaline Phytase Protein Structures Expressed in E. coli

Background: Degradation of phytic acid to inorganic phosphate in domestic animals’ diets requires thermostable phytase. Although Basillus subtilis phytase shows a potential to be degraded phytate complex in high temperature, the enzyme activities and yields need to be increased to make them possible for industrial application. Methods: The phytase gene from Bacillus subtilis DR8886 was...

متن کامل

Production and Partial Characterization of an Extracellular Phytase Produced by Muscodor sp. under Submerged Fermentation

In most of the raw materials of plant origin used in animal feed, a portion of the phosphorus is stored as phytic acid or phytate. Phytate is the main storage form of phosphorus in vegetables but is not readily assimilated into food at low concentrations of the enzyme phytase. In addition to making phosphorous unavailable, phytate binds divalent cations such as calcium, copper, magnesium, iron,...

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

برای دانلود 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

عنوان ژورنال:

دوره 2013  شماره 

صفحات  -

تاریخ انتشار 2013