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http://dx.doi.org/10.4014/jmb.1504.04028

Characterization of a Recombinant Thermostable Arylsulfatase from Deep-Sea Bacterium Flammeovirga pacifica  

Gao, Chao (XingHuaLing District Food and Drug Administration)
Jin, Min (State Key Laboratory Breeding Base of Marine Genetic Resource,Third Institute of Oceanography, SOA)
Yi, Zhiwei (State Key Laboratory Breeding Base of Marine Genetic Resource,Third Institute of Oceanography, SOA)
Zeng, Runying (State Key Laboratory Breeding Base of Marine Genetic Resource,Third Institute of Oceanography, SOA)
Publication Information
Journal of Microbiology and Biotechnology / v.25, no.11, 2015 , pp. 1894-1901 More about this Journal
Abstract
A novel sulfatase gene, ary423 (1,536 bp ORF), encoding a protein of 511 amino acids with a calculated molecular mass of 56 kDa, was identified from Flammeovirga pacifica, which was isolated from deep-sea sediments of west Pacific Ocean. Amino acid sequence analysis revealed that Ary423 possessed a conserved C-X-A-X-R motif, which was recognized as the sulfatase signature. Phylogenetic analysis suggested that Ary423 belonged to arylsulfatases. After heterologous expression in Escherichia coli cells, the recombinant Ary423 was purified with a Ni+ affinity column, and was shown to be highly active at a broad range of temperatures from 30° to 70℃, with maximum activity at 40℃. Furthermore, recombinant Ary423 retained more than 70% and 40% of its maximum activity after 12 h of incubation at 50℃ and 60℃, respectively, exhibiting good thermostability at high temperatures. The optimal pH for Ary423 was determined to be 8.0 and the activity of Ary423 could be slightly enhanced by Mg2+. The recombinant enzyme could hydrolyze sulfate ester bonds in p-nitrophenyl sulfate (NPS) and Asparagus crude polysaccharides with a specific activity of 64.8 U/mg and 25.4 U/mg, respectively. These favorable properties could make Ary423 attractive for application in the desulfating process of agar production.
Keywords
Arylsulfatase; deep sea; Flammeovirga pacifica; thermostability; characterization;
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