Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8331701 | International Journal of Biological Macromolecules | 2015 | 8 Pages |
Abstract
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 °C. Interestingly, Algb possessed broader substrate specificity. It showed activities toward both polyM (poly β-d-mannuronate) and polyG (poly α-l-guluronate). Furthermore, Km 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.
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Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Benwei Zhu, Haidong Tan, Yuqi Qin, Qingsong Xu, Yuguang Du, Heng Yin,