Construction of a bioreactor to produce special breakdown products of phytate.
Escherichia coli phytase was covalently immobilized on NHS-activated Sepharose High Performance. The pH dependence of the phytase activity was not influenced by immobilization, whereas stability against heat treatment was enhanced as a consequence of immobilization. Compared to the free phytase the immobilized enzyme exhibits the same excellent substrate specifity, but showed an increased Km-value. Using the immobilized phytase in a packed-bed bioreactor makes special isomers of the lower myo-inositol phosphate esters available. The major isomers formed were identified as I(1,2,3,4,5)P5, I(2,3,4,5)P4, I(2,4,5)P3 and I(2,5)P2.
Greiner
R
R
Centre for Molecular Biology, Federal Research Centre for Nutrition, Karlsruhe, Germany.
Konietzny
U
U
D010832:6-Phytase / Q000378:metabolism*; D019149:Bioreactors; D001709:Biotechnology; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D004926:Escherichia coli / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D007295:Inositol Phosphates / Q000378:metabolism; D007700:Kinetics; D010833:Phytic Acid / Q000378:metabolism*; D013696:Temperature
D004800:Enzymes, Immobilized; D007295:Inositol Phosphates; D010833:Phytic Acid; D010832:6-Phytase