Purification and properties of a phytase from rye

被引:58
作者
Greiner, R [1 ]
Konietzny, U [1 ]
Jany, KD [1 ]
机构
[1] Fed Res Ctr Nutr, Ctr Mol Biol, D-76131 Karlsruhe, Germany
关键词
D O I
10.1111/j.1745-4514.1998.tb00236.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 of a 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 mu M 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 1(1, 2, 3, 4, 5)P(5) and 1(2, 3, 4, 5)P(4). Consequently, this enzyme is a 6-phytase (EC 3.1.3.26).
引用
收藏
页码:143 / 161
页数:19
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