Characterization of a novel beta-agarase from marine Alteromonas sp. SY37-12 and its degrading products.

The phenotypic and agarolytic features of an unidentified marine bacteria isolated from the southern ocean of China was studied. The strain was gram-negative, aerobic, and polarly flagellated. It was identified as the genus Alteromonas according to its morphological and physiological characterization. In solid agar, the isolate produced a diffusible agarase that caused agar softening around the colonies. An extracellular agarase was purified by the procedure of ammonium sulfate precipitation, gel filtration on Sephacryl S-100HR, and ion-exchange chromatography on diethylaminoethyl-Sepharose. The purified protein exhibited a single band on SDS-PAGE with a molecular mass of 39.5 kDa. The enzyme hydrolyzed the beta-1,4-glycosidic linkages of agar, yielding neoagarotetraose and neoagarohexaose as the main products. The optimum reaction temperature of the agarase was 35 degrees C, with a narrow range from 30 to 45 degrees C. The enzyme activity reached the maximum at pH 7.0 and in the presence of 2% NaCl. Molecular mass and degrading products showed that the agarase from Alteromonas sp. SY 37-12 was much different from those previously reported.