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Characterization of alginate lyase (ALYII) from Pseudomonas sp. OS-ALG-9 expressed in recombinant Escherichia coli

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Abstract

An alginate lyase named ALYII was purified to homogeneity from Escherichia coli JM109 carrying a recombinant plasmid, pJK26 harbouring the alyII gene from Pseudomonas sp. OS-ALG-9 by column chromatography with DEAE-cellulose, CM-Sephadex C-50, butyl-Toyopearl 650 M and isoelectric focusing. The molecular size of the purified ALYII was estimated to be 79 kDa by SDS-PAGE and its pI was 8.3. The enzyme was most active at pH 7.0 and 30 °C. Its activity was completely inhibited by Hg2+. The enzyme was poly β-D-1, 4-mannuronate-specific rather than β-D-1, 4-guluronate-specific and it showed a promotion effect in alginate degradation by combination with ALY, an another poly β-D-1, 4-mannuronate-specific alginate lyase from the same strain.

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Kraiwattanapong, J., Motomura, K., Ooi, T. et al. Characterization of alginate lyase (ALYII) from Pseudomonas sp. OS-ALG-9 expressed in recombinant Escherichia coli. World Journal of Microbiology and Biotechnology 15, 105–109 (1999). https://doi.org/10.1023/A:1008891100111

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