Kiko Fujimori, Sotaro Fujii, Lisa Lisdiana, Satoshi Wakai, Hisashi Yagi, Yoshihiro Sambongi
Deep-sea Shewanella violacea 5′-nucleotidase (SVNTase) activity exhibited higher NaCl tolerance than that of a shallow-sea Shewanella amazonensis homologue (SANTase), the sequence identity between them being 70.4%. Here, SVNTase exhibited higher activity than SANTase with various inorganic salts, similar to the difference in their NaCl tolerance. In contrast, SVNTase activity decreased with various organic solvents, while SANTase activity was retained with the same concentrations of the solvents. Therefore, SVNTase is more robust than SANTase with inorganic salts, but more vulnerable with organic solvents. As to protein stability, SANTase was more stable against organic solvents and heat than SVNTase, which correlated with the differences in their enzymatic activities. We also found that SANTase retained higher activity for three weeks than SVNTase did in the presence of glycerol. These findings will facilitate further application of these enzymes as appropriate biological catalysts under various harsh conditions. © 2019 Japan Society for Bioscience, Biotechnology, and Agrochemistry
Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima, Japan; Department of Biology, Universitas Negeri Surabaya, Kampus Unesa Ketintang, Surabaya, Indonesia; Graduate School of Science, Technology, and Innovation, Kobe University, Kobe, Japan; Department of Chemistry and Biotechnology, Graduate School of Sustainability Science, Tottori University, Tottori, Japan; Center for Research on Green Sustainable Chemistry, Tottori University, Tottori, Japan
