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Isolation and Characterization of an Agarase-Producing Bacterial Strain, Alteromonas sp. GNUM-1, from the West Sea, Korea
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  • Isolation and Characterization of an Agarase-Producing Bacterial Strain, Alteromonas sp. GNUM-1, from the West Sea, Korea
  • Isolation and Characterization of an Agarase-Producing Bacterial Strain, Alteromonas sp. GNUM-1, from the West Sea, Korea
저자명
Kim. Jonghee,Hong. Soon-Kwang
간행물명
Journal of microbiology and biotechnology
권/호정보
2012년|22권 12호|pp.1621-1628 (8 pages)
발행정보
한국미생물생명공학회
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정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

The agar-degrading bacterium GNUM-1 was isolated from the brown algal species Sargassum serratifolium, which was obtained from the West Sea of Korea, by using the selective artificial seawater agar plate. The cells were Gram-negative, $0.5-0.6{mu}m$ wide and $2.0-2.5{mu}m$ long curved rods with a single polar flagellum, forming nonpigmented, circular, smooth colonies. Cells grew at $20^{circ}C-37^{circ}C$, between pH 5.0 and 9.0, and at 1-10% (w/v) NaCl. The DNA G+C content of the GNUM-1 strain was 45.5 mol%. The 16S rRNA sequence of the GNUM-1 was very similar to those of Alteromonas stellipolaris LMG 21861 (99.86% sequence homology) and Alteromonas addita $R10SW13^T$(99.64% sequence homology), which led us to assign it to the genus Alteromonas. It showed positive activities for agarase, amylase, gelatinase, alkaline phosphatase, esterase (C8), lipase (C14), leucine arylamidase, valine arylamidase, ${alpha}$-chymotrypsin, acid phosphatase, naphthol-AS-BI-phosphohydrolase, ${alpha}$-galactosidase, ${eta}$-galactosidase, ${eta}$-glucosidase, catalase, and urease. It can utilize citrate, malic acid, and trisodium citrate. The major fatty acids were summed feature 3 (21.5%, comprising $C_{16:1}{omega}7c/iso-C_{15:0}$ 2-OH) and C16:0 (15.04%). On the basis of the variations in many biochemical characteristics, GNUM-1 was considered as unique and thus was named Alteromonas sp. GNUM-1. It produced the highest agarase activity in modified ASW medium containing 0.4% sucrose, but lower activity in rich media despite superior growth, implying that agarase production is tightly regulated and repressed in a rich nutrient condition. The 30 kDa protein with agarase activity was identified by zymography, and this report serves as the very first account of such a protein in the genus Alteromonas.