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Current Microbiology

, Volume 47, Issue 4, pp 0290–0294 | Cite as

Purification and Characterization of a Phytase from Pseudomonas syringae MOK1

  • Jaie Soon Cho
  • Chang Whan Lee
  • Seung Ha Kang
  • Jae Cheon Lee
  • Jin Duck Bok
  • Yang Soo Moon
  • Hong Gu Lee
  • Sung Chan Kim
  • Yun Jaie Choi
Article

Abstract

A phytase (EC 3.1.3.8) from Pseudomonas syringae MOK1 was purified to apparent homogeneity in two steps employing cation and an anion exchange chromatography. The molecular weight of the purified enzyme was estimated to be 45 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. The optimal activity occurred at pH 5.5 and 40°C. The Michaelis constant (K m ) and maximum reaction rate (Vmax) for sodium phytate were 0.38 mM and 769 U/mg of protein, respectively. The enzyme was strongly inhibited by Cu2+, Cd2+, Mn2+, and ethylenediaminetetraacetic acid (EDTA). It showed a high substrate specificity for sodium phytate with little or no activity on other phosphate conjugates. The enzyme efficiently released orthophosphate from wheat bran and soybean meal.

Keywords

Pseudomonas Bran Anion Exchange Ethylenediaminetetraacetic Acid Soybean Meal 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag New York Inc. 2003

Authors and Affiliations

  • Jaie Soon Cho
    • 1
  • Chang Whan Lee
    • 2
  • Seung Ha Kang
    • 1
  • Jae Cheon Lee
    • 1
  • Jin Duck Bok
    • 2
  • Yang Soo Moon
    • 1
  • Hong Gu Lee
    • 1
  • Sung Chan Kim
    • 1
  • Yun Jaie Choi
    • 1
  1. 1.School of Agricultural Biotechnology, College of Agriculture and Life Science, Seoul National University, 441-744, Suweon, KoreaKR
  2. 2.Choong Ang Biotech Co., Ltd., 833-6 Wonsi-Dong, Ansan-City, Kyunggi-Do, KoreaKR

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