High Impact Factor : 4.396 icon | Submit Manuscript Online icon |

Bacillus cereus 10072 Phytase - Detection, Purification, Characterization and Physiological Role


Utkarsh Jain , Department of Microbiology, TMDCRC, Moradabad, U.P.; Nidhi Chauhan, Amity Institute of Nanotechnology, Amity University, Noida- 201303, India


Phytase, Iso electric focusing, Bacillus cereus, Enzyme characterization, Animal feed


Phytase from Bacillus cereus MTCC 10072 was purified about 10.75 fold to apparent homogeneity with a recovery of 34% referred to the phytase activity in the crude extract. The monomeric enzyme displayed molecular weight of 45 KDa and showed maximum activity at temperature 60 ºC and pH 6.5. Iso electric point of the purified enzyme was found to be 5.6. Substrate specificity studies showed it is highly specific to its substrate and maximum relative activity of 128% was obtained with calcium phytate. Activity was unaffected or moderately stimulated by a range of metal ions with only Ca2+ exerting (118%) stimulatory effect. The enzyme is significantly thermo stable at 60 ºC and retains a significantly greater proportion of maximal activity at physiological temperatures. This may render it of industrial interest. Further to check the applicability of the enzyme effect of different doses of crude enzyme (10, 25, 50 and 100 units) in dephosphorylation of animal feed was evaluated. Up to 66 h of incubation, the animal feed was monitored for the released inorganic phosphate content present in the feed. An enzyme dose of 100U and 50U of crude phytase enzyme per flask were found suitable to liberate enough amount of inorganic phosphorus in case of poultry and pig feed respectively.

Other Details

Paper ID: IJSRDV2I9004
Published in: Volume : 2, Issue : 9
Publication Date: 01/12/2014
Page(s): 14-19

Article Preview

Download Article