Journal
EXTREMOPHILES
Volume 17, Issue 6, Pages 931-939Publisher
SPRINGER JAPAN KK
DOI: 10.1007/s00792-013-0575-z
Keywords
Halococcus; Thermophilic; Halophilic; beta-agarase
Categories
Funding
- Ministry of Education, Culture, Sports, Science and Technology (MEXT)
- Grant for the Strategic Development of Advanced Science and Technology [S1101017]
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An agar-degrading archaeon Halococcus sp. 197A was isolated from a solar salt sample. The agarase was purified by hydrophobic column chromatography using a column of TOYOPEARL Phenyl-650 M. The molecular mass of the purified enzyme, designated as Aga-HC, was similar to 55 kDa on both SDS-PAGE and gel-filtration chromatography. Aga-HC released degradation products in the order of neoagarohexose, neoagarotetraose and small quantity of neoagarobiose, indicating that Aga-HC was a beta-type agarase. Aga-HC showed a salt requirement for both stability and activity, being active from 0.3 M NaCl, with maximal activity at 3.5 M NaCl. KCl supported similar activities as NaCl up to 3.5 M, and LiCl up to 2.5 M. These monovalent salts could not be substituted by 3.5 M divalent cations, CaCl2 or MgCl2. The optimal pH was 6.0. Aga-HC was thermophilic, with optimum temperature of 70 A degrees C. Aga-HC retained approximately 90 % of the initial activity after incubation for 1 hour at 65-80 A degrees C, and retained 50 % activity after 1 hour at 95 A degrees C. In the presence of additional 10 mM CaCl2, approximately 17 % remaining activity was detected after 30 min at 100 A degrees C. This is the first report on agarase purified from Archaea.
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