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

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Abstract

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 β-1,4-glycosidic linkages of agar, yielding neoagarotetraose and neoagarohexaose as the main products. The optimum reaction temperature of the agarase was 35°C, with a narrow range from 30 to 45 °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.

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Correspondence to Haijin Mou.

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Wang, J., Mou, H., Jiang, X. et al. Characterization of a novel β-agarase from marine Alteromonas sp. SY37–12 and its degrading products. Appl Microbiol Biotechnol 71, 833–839 (2006). https://doi.org/10.1007/s00253-005-0207-3

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  • DOI: https://doi.org/10.1007/s00253-005-0207-3

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