NDLI: Isolation and Molecular Characterization of Thermostable Phytase from Bacillus subtilis (BSPhyARRMK33)

Content Provider	Springer Nature Link
Author	Reddy, Chinreddy Subramanyam Achary, V. Mohan Murali Manna, Mrinalini Singh, Jitender Kaul, Tanushri Reddy, Malireddy K.
Copyright Year	2015
Abstract	The thermostable phytase gene was isolated from Bacillus subtilis ARRMK33 (BsPhyARRMK33). The gene has an ORF of 1152 bp and that encodes a protein of 383 amino acids. Sequence analysis showed high homology with Bacillus sp. phytase proteins, but no similarity was found with other phytases. SDS-PAGE analysis exhibited a predicted molecular mass of 42 kDa. Homology modeling of BsPhyARRMK33 protein based on Bacillus amyloliquefaciens crystal structure disclosed its β-propeller structure. BsPhyARRMK33 recombinant plasmid in pET-28a(+) was expressed in Rosetta gami B DE3 cells and the maximum phytase activity 15.3 U mg$^{−1}$ obtained. The enzyme exhibits high thermostability at various temperatures and broad pH ranges. The recombinant protein retained 74 % of its original activity after incubation at 95 °C for 10 min. In the presence of Ca$^{2+}$, the recombinant phytase activity was maximal where as it was inhibited by EDTA. The optimal pH and temperature for the recombinant phytase activity is achieved at 7.0 and 55 °C, respectively. Thermostable nature and wide range of pH are promising features of recombinant BsPhyARRMK33 protein that may be employed as an efficient alternative to commercially known phytases and thereby alleviate environmental eutrophication.
Starting Page	3058
Ending Page	3067
Page Count	10
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	175
Issue Number	6
e-ISSN	15590291
Language	English
Publisher	Springer US
Publisher Date	2015-01-15
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Bacillus subtilis Phytase Thermostable Feed additive Phytate Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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