The phytase of wheat

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Abstract
Some properties of wheat phytase were studied using both wholemeal and a partially purified prepn. The opt. pH of the enzyme is 5.15, opt. temp. 55[degree], and Michaelis constant (Km) 0.3 x 10-3 [image]: The enzyme is activated by Mg at an opt. concn. of 0.002 [image]. A procedure was worked out for the partial purification (about 20-fold on a dry matter basis) of the enzyme from wholemeal. The distr. of phytase among the anatomical fractions of the wheat grain was detd. An increase of 6.5-fold in the phytase activity was observed when a soft wheat (Cappelle Deprez) germinates. The phytase activity of a number of different wheats was detd. Hard wheats have a higher activity than softs wheats. The influence of a number of inorganic and organic salts on phytase action was detd. Heavy metal salts completely inhibit the enzyme probably by removing the phytate from soln. With the enzyme in soln. the rate of thermal inactivation does not follow the unimolecular expression but an approx. value for the heat of inactivation is 41,000 cal.

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