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Comparative Study
. 2003 Aug;25(15):1231-4.
doi: 10.1023/a:1025020309596.

Isolation and characterization of a phytase with improved properties from Citrobacter braakii

Han-Woo Kim  1 , Young-Ok Kim, Jeong-Ho Lee, Kyung-Kil Kim, Yung-Jin Kim
Affiliations
Comparative Study

Isolation and characterization of a phytase with improved properties from Citrobacter braakii

Han-Woo Kim et al. Biotechnol Lett. 2003 Aug.

Abstract

Citrobacter braakii YH-15 produced an intracellular phytase which was purified 12800 fold to homogeneity with the specific activity of 3457 units mg(-1), which is 1.9 times higher than E. coli phytase previously recorded as having the highest specific activity. Its molecular weight was 47 kDa by SDS-PAGE gel. Enzyme activity was optimal at pH 4 and at 50 degrees C. The Km value for sodium phytate was 0.46 mM with a Vmax 6027 U mg(-1). The phytase was resistant to proteases such as trypsin, pepsin, papain, pancreatin, and elastase.

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