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- W160282576 abstract "Extracellular serine proteases were isolated from a soil bacterium, alkalophilic coryneform bacterium TU-19, which have been grown in a liquid medium optimized at 30°C and pH 10.0. Three different sizes, 120 kDa (protease I), 80 kDa (protease II), and 45 kDa (protease III), of serine proteases were purified using Sephadex G-150 and QAE-Sephadex chromatography (Kang et al. 1995. Agric. Chem. Biotech. 38: 534-540). SDS-PAGE showed that the 120 kDa protease was degraded into the 80 kDa protease in 20 mM Tris-HCl (pH 8.0) buffer solution. This degradation was enhanced in the presence of 0.5 M NaCI and 5 mM EDTA, but was inhibited in the presence of 5 mM CaCl 2 . These results indicated that the Ca 2+ ion seems to stabilize the 120 kDa protease like other proteases derived from Bacillus species. The NH 2 -terminal amino acid sequences of the 10 residues of both proteases were completely identical: Met-Asn-Thr-Gln-Asn-Ser-Phe-Leu-Ile-Lys. In contrast to this, the 80 kDa protease has 1.5 times higher specific activity than the 120 kDa protease does (Kang et al. 1995. Agric. Chem. Biotech. 38: 534-540). Therefore the C-terminal of the 120 kDa protease seems to be autolyzed to the 80 kDa protease but this autolysis did not decrease the protease activity. Optimum pH and temperature of both 80 kDa and 120 kDa proteases were pH 10.5 and 45°C, respectively, and pH and thermal stability were almost identical. Several divalent ions except the Fe 2+ ion showed similar effects on activities of both proteases, which are similarly resistant to three different detergents." @default.
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- W160282576 date "1998-01-01" @default.
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- W160282576 title "Characterization of alkaline serine proteases secreted from the coryneform bacterium TU-19" @default.
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