Purification and characterization of a novel alpha-agarase from a Thalassomonas sp.
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 alpha-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 degrees 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 alpha-agarase, and the final main product was agarotetraose. The enzyme degraded not only agarose but also agarohexaose, neoagarohexaose, and porphyran.
Ohta
Yukari
Y
Japan Agency for Marine-Earth Science and Technology, 2-15 Natsushima, Yokosuka 237-0061, Japan.
Hatada
Yuji
Y
Miyazaki
Masayuki
M
Nogi
Yuichi
Y
Ito
Susumu
S
Horikoshi
Koki
K
D020563:Gammaproteobacteria / Q000145:classification / Q000201:enzymology* / Q000254:growth & development; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D010802:Phylogeny
D006026:Glycoside Hydrolases; C019624:agarase