Abstract
Phytase (myo-inositol hexakisphosphate phosphohydrolase) has been purified about 2,000-fold from ungerminated rye with a recovery of 6%. The enzyme behaves as a monomeric protein ofa molecular mass of about 67 kDa. Optimal pH for the degradation of phytate has been found at pH 6.0 and 45C. Kinetic parameters for the hydrolysis of Na-phytate are K M 300 μM and k cat 358 s -1 at 35C and pH 6. 0. The rye enzyme exhibits a broad affinity for various phosphorylated compounds and hydrolyses phytate in a stepwise manner; the pentakis- and tetrakisphosphate were identified as I(1,2,3,4,5)P 5 and I(2,3,4,5)P 4 . Consequently, this enzyme is a 6-phytase (EC 3.1.3.26).
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