AI Article Synopsis
- The beta-propeller phytase (BPP) from Pseudomonas sp. FB15 has a unique N-terminal domain not found in other BPPs, which may enhance its enzyme properties.
- A fusion of this N-terminal domain with the BPP from Bacillus sp. SJ-10 (resulting in FUSJ-10phy) showed improved turnover rate and catalytic efficiency, along with a lower optimal temperature compared to the wild-type BPP.
- Additional experiments with BPP from Bacillus sp. SJ-48 also demonstrated similar increases in efficiency and activity at lower temperatures when fused with the PSphy N-terminal domain.
Article Abstract
The beta-propeller phytase (BPP) is an enzyme that hydrolyzes phyate to release inorganic phosphorus. The BPP produced by Pseudomonas sp. FB15 (PSphy) possesses an additional N-terminal domain that is not present in BPP produced by other Bacillus species. In this study, BPP produced by Bacillus sp. SJ-10 (SJ-10phy) was fused with the N-terminal domain of PSphy and the enzymatic properties of the resulting fusion protein (FUSJ-10phy) were investigated. FUSJ-10phy exhibited an optimal temperature that was 10 °C lower than that of the wild-type enzyme. A comparison of kinetic parameters showed that the turnover rate of FUSJ-10phy was 2.39-fold higher than that of SJ-10phy, representing a 1.79-fold increase in catalytic efficiency. In addition, BPP produced by Bacillus sp. SJ-48 has relatively low sequence similarity with SJ-10phy, was fused with N-terminal domain (FUSJ-48phy). FUSJ-48phy also increased catalytic efficiency and changed the optimal temperature. These results indicate that, when fused to other BPPs, the N-terminal domain of PSphy increases catalytic efficiency and enzyme activity at lower temperatures.
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| http://dx.doi.org/10.1016/j.enzmictec.2019.04.002 | DOI Listing |
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