Related Experiment Video
Updated: Apr 17, 2026

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
Published on: April 22, 2016
Characterization of a new endo-type alginate lyase from Vibrio sp. W13
Benwei Zhu1, Haidong Tan2, Yuqi Qin3
1Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, PR China; University of Chinese Academy of Sciences, Beijing 100049, PR China.
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, 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.

