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Purification and characterization of β-agarase from marine bacterium Bacillus cereus ASK202

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Abstract

Extracellular agarase of Bacillus cereus ASK202 was purified 32-fold, giving a single band on PAGE with activity staining. The Mr of purified agarase was determined as 90 kDa by SDS-PAGE. The N-terminal amino acid was sequenced and the sequence did not show homology to any other known agarases. The optimum pH and temperature were 7.0 and 40 °C, respectively. This enzyme was found to be a β-agarase which catalyzed the hydrolysis of the β-1,4 linkage of agarose to yield neoagarohexaose, neoagarotetraose and neoagarobiose.

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Kim, B.J., Kim, H.J., Duck Ha, S. et al. Purification and characterization of β-agarase from marine bacterium Bacillus cereus ASK202. Biotechnology Letters 21, 1011–1015 (1999). https://doi.org/10.1023/A:1005604618242

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  • DOI: https://doi.org/10.1023/A:1005604618242

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