A novel β-propeller phytase from the dioxin-degrading bacterium Sphingomonas wittichii RW-1
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β-propeller phytase-like sequences (BPP-like sequences) are widespread in the microbial world and have been found in the sequenced genomes of aquatic, soil, and plant bacteria. Exploring NCBI microbial genome database for putative genes encoding phytase, a BPP-like sequence from Sphingomonas wittichii RW-1 (Sequence ID: CP000699.1), known for its capacity of degrading polychlorinated dibenzo-p-dioxins and dibenzofurans, was recognized. The putative phytase gene (phySw) was amplified with specific primers, cloned, and overexpressed in Escherichia coli and the catalytic properties of the recombinant PhySw protein were analyzed. The results show that phySw encodes an enzyme with the properties of β-propeller phytases: it requires the presence of Ca2+ ions, it is optimally active at 55 °C, and it has a pH optimum of 6.0 with good activity in the range 6.0–8.0. Furthermore, the enzyme exhibits a good thermostability, recovering 68% of its original activity after treatment at 80 °C for 10 min, and shows a good substrate specificity for phytic acid. These properties render this enzyme a candidate as an animal feed additive (e.g., for aquaculture industry). The isolation of phytases from a hydrocarbon-utilizing microorganism also opens new scenarios for their possible application in combating oil pollution.
KeywordsSphingomonas wittichii Phytate β-propeller phytase Heterologous expression Thermostability Animal feed Bioremediation
The authors are also grateful to Technopole SITEIA-Parma (Regione Emilia-Romagna) and Prof Nelson Marmiroli for allowing access to technical infrastructures.
This research was in part supported by funding to Prof. Anna Maria Sanangelantoni from FIL of the University of Parma (Local Funding for Research).
Compliance with ethical standards
No animal and/or human were employed in this work.
Conflict of interest
The authors declare that they have no conflict of interest.
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