Biochemical characterization of phytase purified from Aspergillus niger S2
  • Article Type: Research Article
  • Eurasian Journal of Biosciences, 2019 - Volume 13 Issue 1, pp. 99-103
  • Published Online: 20 Mar 2019
  • Article Views: 177 | Article Download: 93
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AMA 10th edition
In-text citation: (1), (2), (3), etc.
Reference: Sandhya A, Sridevi A, Suvarnalathadevi P. Biochemical characterization of phytase purified from Aspergillus niger S2. Eurasia J Biosci. 2019;13(1), 99-103.

APA 6th edition
In-text citation: (Sandhya et al., 2019)
Reference: Sandhya, A., Sridevi, A., & Suvarnalathadevi, P. (2019). Biochemical characterization of phytase purified from Aspergillus niger S2. Eurasian Journal of Biosciences, 13(1), 99-103.

Chicago
In-text citation: (Sandhya et al., 2019)
Reference: Sandhya, Arani, Ayla Sridevi, and Pallipati Suvarnalathadevi. "Biochemical characterization of phytase purified from Aspergillus niger S2". Eurasian Journal of Biosciences 2019 13 no. 1 (2019): 99-103.

Harvard
In-text citation: (Sandhya et al., 2019)
Reference: Sandhya, A., Sridevi, A., and Suvarnalathadevi, P. (2019). Biochemical characterization of phytase purified from Aspergillus niger S2. Eurasian Journal of Biosciences, 13(1), pp. 99-103.

MLA
In-text citation: (Sandhya et al., 2019)
Reference: Sandhya, Arani et al. "Biochemical characterization of phytase purified from Aspergillus niger S2". Eurasian Journal of Biosciences, vol. 13, no. 1, 2019, pp. 99-103.

Vancouver
In-text citation: (1), (2), (3), etc.
Reference: Sandhya A, Sridevi A, Suvarnalathadevi P. Biochemical characterization of phytase purified from Aspergillus niger S2. Eurasia J Biosci. 2019;13(1):99-103.

Abstract

Background: Phytic acid is the large reservoir of phosphorous of plant origin feed of monogastric animals. These animals are incapable of metabolizing phytic acid due to lack of phytase enzyme production. Phytases are a group of enzymes which are involved in hydrolyzing phytic acid and releasing inorganic phosphate Microorganisms are the main sources of phytases especially purified from filamentous fungi Aspergillus nigerS2.
Materials and Methods: In the present study, a three step purification study of phytase from Aspergillus niger S2 was done by using Sephadex G-50. The active fractions pooled after chromatography step was used for molecular mass determination through sodium dodecyl sulphate- poly acrylamide gel electrophoresis (SDSPAGE). Phytase activity was determined at different pH between 3.0 and 8.0. The effect of temperature on enzyme activity was studied of temperature range of 30-60 ºC. The action of the enzyme on several phosphorylated substrates was tested at concentrations of 3mM. The phytase enzyme function was tested on digestion of plant material.
Results: The molecular mass of A. niger phytase S2was also found to be 50kDa. The enzyme showed optimal pH at 5.0. The enzyme showed maximum activity at 400C. The enzyme showed high substrate affinity towards sodium phytate. The purified enzyme activity on digestion of grass and hay showed positive results with increased protein content, reducing sugar and phosphate.
Conclusion: The purified enzyme of the present study with these specifications can able to play a vital role in feed industry as a feed supplement in order to metabolize phytic acid and hence reduce soil pollution and eutrophication.

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