Isolation and Characterization of Phytase from Chicken Manure Bacteria

Mega Pratiwi Irawan, Zeily Nurachman


Cereals in animal feed contain anti-nutrients of phytic acid that has capability of chelating proteins and cations. Phytasecan be employed to reduce phytic acid through hydrolyzing phytic acid into free phosphate group and lower derivate ofinositol phosphate. The aim of the study was to isolate and characterize phytase obtained from chicken manure bacteria.The study included the screening of phytase-producing bacteria from chicken manure, the homology analysis of bacterium,and the determination of phytase activity. Phytase activity was measured from concentration of free phosphate. The resultsshowed that one phytase-producing isolate obtained from chicken manure grew in the medium containing 5% rice branextract at 37°C for 5 d. Based on a phylogeny is tree analysis of the genes related to 16S rRNA, the isolate was identified asAcinetobacter sp. TZ1. The extracellular phytase expressed by Acinetobacter sp. TZ1 exhibited optimum reactions at pH5 and 50°C. The enzyme showed activity of 64,6 nmol mL–1min–1 and specific activity of 236 nmol min–1mg–1. Relativemolecular mass of phytase TZ1 was ~35 kDa. Phytase obtained is potential to improve animal feed quality by hydrolyzingphytic acid.


chicken manure bacteria, phytase, rice bran

Full Text:



Bae, H.D., Yanke, L.J., Cheng, K.J & Selinger, L.B. 1999. A novel staining method for detecting phytase activity. J Microbiol Methodes (39): 17–22.

Bohn, L., Meyer, A.S & Rasmussen, S.K. 2008. Phytate: impact on environment and human nutrition. A challenge for molecular breeding. J Zhejiang Univ SCIENCE B (3): 165–191.

Chang, H.C., Wei, Y.F., Dijkshoorn, L., Vaneechoutee, M., Tang, C.T & Chang, T.C. 2005. Species-level identification of Acinetobacter calcoacitecus- Acinetobacter baumanii complex by sequence analysis of the 16S-23S rRNA gene spacer region. J Clinical Microbiol (43): 1632–1639.

Fiske, C.H & Subbarow, Y. 1925. The colometric determination of phosphorus. J Biol Chem (66): 375– 400.

Kerovuo, J., Lauraeus, M., Nurminen, P., Kalkkinen, N & Apajalahti, J. 1998. Isolation, characterization, molecular gene cloning, and sequencing of a novel phytase from Bacillus subtilis. Appl Environ Microbiol 2079–2085.

Kerovuo, J., Rouvinen, J & Hatzack, F. 2000. Analysis of myo–inositol hexakisphosphate hydrolysis by Bacillus phytase : indication of a novel reaction mechanism. Biochem J (352): 623–628.

Koma, D., Hasumi, F., Yamamoto, E., Ohta, T., Chung, S.Y & Kubo, M. 2001. Biodegradation of long-chain n- paraffin from waste oil of car engine by Acinetobactor sp. J Biosci Bioeng (91): 94–96.

Lei, X.G & Porres, J.M. 2003. Phytase enzymology, application, and biotechnology. Biotechnol Letter (25): 1787–1794.

Liu, B.L., Rafiq, A., Tzeng, Y.M & Rob, A. 1998. The induction and characteriszation of phytase and beyond. Enzyme and Microbial Technol (22): 415– 424.

Raghavendra, P& Halami, P.M. 2009. Screening, selection and characterization of phytic acid degrading bacteria from chicken intestine. Intl J Food Microbiol (133): 129–134.

Sakai, Y., Maeng, J.H., Tani, Y & Kato, N. 1994. Use of long-chain n-alkanes (C13 – C44) by an isolate Acinetobacter sp. M-1. Biosci Biotech Biochem (58): 2128–2130.

Tremaroli, V & Bäckhed, F. 2012. Functional interactions between the gut microbiota and host metabolism. NATURE (489): 242–249.

Visca, P., Seifert, H & Towner, K.J. 2011. Acinetobacter infection – an emerging threat to human health. IUBMB Life (63): 1048–1054.

Palacios, M.C., Haros, M., Sanz, Y & Rosell, C.M. 2008. Selection of lactic acid bacteria with high phytate degrading activity for application in whole wheat breadmaking. LWT (41): 82–92.



  • There are currently no refbacks.

Copyright (c) 2015 Mega Pratiwi Irawan, Zeily Nurachman

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.