This work was a cooperative investigation between the Agricultural Research Service, USDA, and the Wisconsin Agricultural Experiment Station, Madison. Mention of a trademark or proprietary product does not constitute a guarantee or warranty of the product by the U. S. Department of Agriculture and does not imply its approval to the exclusion of other products that may also be suitable. Research supported in part by USDA Cooperative Agreement 12-14-100-10,888, and by the
The phytase (EC 3.1.3.8.) of Sanilac Navy Beans was extracted with 2% CaCl, and purified by ammonium sulfate fractionation and DEAEcellulose chromatography. The enzyme showed an optimum pH of 5.3 and Km of 0.018 mM with phytic acid as substrate. The optimum temperature was 50°C. The activation energy of the enzymic hydrolysis of phytic acid was 11,500 Cal/mole and the inactivation energy of the enzyme 55,800 Cal/mole. The purified phytase showed broad specificity. This enzyme may be described as a nonspecific phosphomonoesterase with phytase and potent pyrophosphatase activities. It was inhibited by high concentrations of phytic acid. The activity was increased by about 35% in the presence of 1 mM Co++. Soaking of beans in distilled water did not affect their phytic acid content and phytase activity. Germination of the beans resulted in an increase in phytase activity and breakdown of phytic acid.
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