A novel psychrophilic alkaline phosphatase from the metagenome of tidal flat sediments

Researchers have identified and characterized a novel psychrophilic alkaline phosphatase (mAP) from the metagenome of tidal flat sediments in Getbol, Korea. This enzyme, distinct from classical PhoA family members, exhibits high catalytic activity at low temperatures and remarkable thermal instability, with optimal activity at 37°C and complete inactivation by 65°C within 15 minutes. mAP demonstrates broad substrate specificity, efficiently removing terminal phosphates from linearized plasmid DNA, a capability comparable to commercially available alkaline phosphatases. This discovery marks the first thermolabile AP found in cold-adapted marine metagenomes, offering potential applications in molecular biology for dephosphorylation processes.

Lee, D.-H., Choi, S.-L., Rha, E., Kim, S. J., Yeom, S.-J., Moon, J.-H., & Lee, S.-G. (2015). A novel psychrophilic alkaline phosphatase from the metagenome of tidal flat sediments. BMC Biotechnology, 15(1). https://doi.org/10.1186/s12896-015-0115-2