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1. [beta]-propeller phytase hydrolyzes insoluble [Ca.sup.2+]-phytate salts and completely abrogates the ability of phytate to chelate metal ions

Author

Ok-Hee Kim, Young-Ok Kim, Jae-Hoon Shim, Yun-Shin Jung, Woo-Jin Jung, Won-Chan Choi, Heeseob Lee, Sang-Jun Lee, Kyung-Kil Kim, Joong-Huck Auh, Hyeonjin Kim, Jung-Wan Kim, Tae-Kwang Oh, and Byung-Chul Oh

Subjects
Calcium -- Chemical properties, Enzyme binding -- Analysis, Hydrolysis -- Analysis, Isothermal titration calorimetry -- Usage, Phytic acid -- Chemical properties, Biological sciences, Chemistry
Abstract

Isothermal titration calorimetry is used to determine the stoichiometry, affinity, and thermodynamics of binding interactions of phytate, an antinutritional factor with biologically important metal cations. The multiple [Ca.sup.2+]-binding sites found in phytate which forms insoluble tricalcium- or tetracalcium-phytate salts over a wide pH range could find new insights into the potential application of [beta]-propeller phytase from Hahella chejuensis (HcBPP) in enhancing the bioavailability and absorption of divalent cations.

Published
2010

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