• Microbiology and Biotechnology Letters
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• v.24 no.2
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• pp.160-165
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• 1996

An alkalophilic bacterium producing alkaline protease(s) was isolated from soil. It was a Gram-positive, non-sporulating, immotile, irregular rod, strictly aerobic, and weak acid-forming bacterium. The morphological, physiological, and biochemical characteristics of the isolate resembled those of the Coryneform bacteria. However, there was not any species within this genera to which this microorganism can be closely matched. Therefore, it is provisionally identified as a Coryneform bacterium TU-19.

• Applied Biological Chemistry
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• v.41 no.5
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• pp.337-341
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• 1998

The morphological and cultural characteristics of alkalophilic Coryneform bacteria TU-19 were investigated at various pHs. This bacterium showed normal growth pattern at $pH\;9.0{\sim}10.0$, but the cell growth was completely inhibited at extreme pH (12.0 or more). Interestingly, at pH 8.0 the morphology of the bacterial cells seems to form convoluted filaments during the exponential growth phase while at pH 10.0, the optimal pH for the growth of this organism, the bacteria grew with variable paired or single forms, and straight rods during growth stages. Growing in alkaline media $(pH\;9.0{\sim}11.0)$, it adjusted the pH of the culture media to around pH 8.5 by itself.

• Journal of Microbiology and Biotechnology
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• v.8 no.6
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• pp.639-644
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• 1998

Extracellular serine proteases were isolated from a soil bacterium, alkalophilic coryneform bacterium TU-19, which have been grown in a liquid medium optimized at 3$0^{\circ}C$ and pH 10.0. Three different sizes, 120 kDa (protease I), 80 kDa (protease II), and 45 kDa (protease III), of serine pro teases 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-HCI (pH 8.0) buffer solution. This degradation was enhanced in the presence of 0.5 M NaCl 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. Chern. 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 $45^{\circ}C$, 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.