Purification and Characterization of a Bacterial Phytase Whose Properties Make it Exceptionally Useful as a Feed Supplement |
| |
Authors: | Ralf Greiner Abd-ElAziem Farouk |
| |
Institution: | Centre for Molecular Biology, Federal Research Centre for Nutrition and Food, Haid-und-Neu-Strasse 9, D-76131, Karlsruhe, Germany. ralf.greiner@bfel.de |
| |
Abstract: | A periplasmatic phytase from a bacterium isolated from Malaysian waste water was purified about 173-fold to apparent homogeneity
with a recovery of 10% referred to the phytase activity in the crude extract. It behaved as a monomeric protein with a molecular
mass of about 42 kDa. The purified enzyme exhibited a single pH optimum at 4.5. Optimum temperature for the degradation of
phytate was 65°C. The kinetic parameters for the hydrolysis of sodium phytate were determined to be K
M = 0.15 mmol/l and k
cat = 1164 s−1 at pH 4.5 and 37°C. The purified enzyme was shown to be highly specific. Among the phosphorylated compounds tested, phytate
was the only one which was significantly hydrolysed. Some properties such as considerable activity below pH 3.0, thermal stability
and resistance to pepsin make the enzyme attractive for an application as a feed supplement. |
| |
Keywords: | Phytate-degrading enzyme phytate phytase waste– water bacterium |
本文献已被 PubMed SpringerLink 等数据库收录! |