Purification and characterization of a bacterial phytase whose properties make it exceptionally useful as a feed supplement
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 enzy...
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| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
Springer
2007
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| Subjects: | |
| Online Access: | http://irep.iium.edu.my/14233/1/Purification_and_Characterization.pdf http://irep.iium.edu.my/14233/ http://www.springerlink.com/content/d347721083j44772/ |
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| Summary: | 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 KM = 0.15 mmol/l and kcat = 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. |
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