Characterization of alginate lyase (ALYII) from Pseudomonas sp. OS-ALG-9 expressed in recombinant Escherichia coli |
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Authors: | Kraiwattanapong J Motomura K Ooi T Kinoshita S |
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Institution: | (1) Department of Molecular Chemistry, Graduate School of Engineering, Hokkaido University, N-13, W-8, Kita-ku, Sapporo, Hokkaido, 060, Japan |
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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 -D-1, 4-mannuronate-specific rather than -D-1, 4-guluronate-specific and it showed a promotion effect in alginate degradation by combination with ALY, an another poly -D-1, 4-mannuronate-specific alginate lyase from the same strain. |
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Keywords: | Alginate lyase gene expression polymannuronate lyase Pseudomonas sp |
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