An agar-degrading Thalassomonas bacterium, strain JAMB-A33, was isolated from the sediment off Noma Point, Japan, at a depth of 230 m. A novel α-agarase from the isolate was purified to homogeneity from cultures containing agar as a carbon source. The molecular mass of the purified enzyme, designated as agaraseA33, was 85 kDa on both SDS-PAGE and gel-filtration chromatography, suggesting that it is a monomer. The optimal pH and temperature for activity were about 8.5 and 45°C, respectively. The enzyme had a specific activity of 40.7 U/mg protein. The pattern of agarose hydrolysis showed that the enzyme is an endo-type α-agarase, and the final main product was agarotetraose. The enzyme degraded not only agarose but also agarohexaose, neoagarohexaose, and porphyran. © Springer Science+Business Media, Inc. 2005.
CITATION STYLE
Ohta, Y., Hatada, Y., Miyazaki, M., Nogi, Y., Ito, S., & Horikoshi, K. (2005). Purification and characterization of a novel α-agarase from a Thalassomonas sp. Current Microbiology, 50(4), 212–216. https://doi.org/10.1007/s00284-004-4435-z
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