AI Article Synopsis
- Phytase breaks down phytate in grains to release bioavailable inorganic phosphate, but traditional assays for measuring this activity are time-consuming and hazardous.
- The article introduces a new kinetic assay method that uses IP(6)-lysozyme complexes, which simplifies the process and can be adapted for high-throughput testing.
- This method effectively measures phytase activity by monitoring changes in turbidity, while also investigating how different conditions like temperature and salt concentrations affect the assay results.
Article Abstract
Phytase (EC 3.1.3.-) hydrolyzes phytate (IP(6)) present in cereals and grains to release inorganic phosphate (P(i)), thereby making it bioavailable. The most commonly used method to assay phytase, developed nearly a century ago, measures the P(i) liberated from IP(6). This traditional endpoint assay is time-consuming and well known for its cumbersomeness in addition to requiring extra caution for handling the toxic regents used. This article reports a simple, fast, and nontoxic kinetic method adaptable for high throughput for assaying phytase using IP(6)-lysozyme as a substrate. The assay is based on the principle that IP(6) forms stable turbid complexes with positively charged lysozyme in a wide pH range, and hydrolysis of the IP(6) in the complex is accompanied by a decrease in turbidity monitored at 600 nm. The turbidity decrease correlates well to the released P(i) from IP(6). This kinetic method was found to be useful in assaying histidine acid phytases, including 3- and 6-phytases, a class representing all commercial phytases, and alkaline β-propeller phytase from Bacillus sp. The influences of temperature, pH, phosphate, and other salts on the kinetic assay were examined. All salts, including NaCl, CaCl(2), and phosphate, showed a concentration-dependent interference.
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| http://dx.doi.org/10.1016/j.ab.2010.10.034 | DOI Listing |
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