4.7 Article

Characterization of a new endo-type alginate lyase from Vibrio sp W13

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ELSEVIER
DOI: 10.1016/j.ijbiomac.2015.01.053

Keywords

Alginate lyase; Polysaccharide lyase family 7; Vibrio sp.

Funding

  1. National Key Technology Support Program [2013BAB01B01]
  2. Special Fund for Marine Scientific Research [201305015-2]
  3. National Natural Science Foundation of China [31100203]
  4. Development Fund for Collaborative Innovation Center of Glycoscience of Shandong University
  5. Ocean Public Welfare Scientific Research Project, State Oceanic Administration of China [201405003]

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A gene, encoding a new alginate lyase Algb, was identified and cloned from marine bacterium Vibrio sp. W13. The recombinant alginate lyase was characterized followed by being purified on Ni-NTA Sepharose. It exhibited the highest activity (457 U/mg) at pH 8.0 and 30 degrees C Interestingly, Algb possessed broader substrate specificity. It showed activities toward both polyM (poly beta-D-mannuronate) and polyG (poly alpha-L-guluronate). Furthermore, K-m values of Algb toward alginate (0.67 mg/ml) and polyMG (0.50 mg/ml) are lower than those toward polyG (1.04 mg/ml) and polyM (6.90 mg/ml). The TLC and ESI-MS analysis suggested that Algb mainly released oligosaccharides with DP of 2-5 from the four kinds of substrates in an endolytic manner. Therefore, it may be a potent tool to produce alginate oligosaccharides with low DP. (C) 2015 Elsevier B.V. All rights reserved.

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