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Isolation from the marine mollusk Lambis sp. and catalytic properties of an alginate lyase with rare substrate specificity

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Chemistry of Natural Compounds Aims and scope

Homogeneous alginate lyase with rare specificity exhibiting maximum activity at pH 5.0 and temperature range 40–55°C that catalyzed cleavage of 1→4 glycoside bonds between α-L-guluronic acid residues was isolated from liver-pancreas of the marine gastropod mollusk Lambis sp. The alginate lyase was classified as a poly-1→4-α-L-guluronate lyase (EC 4.2.2.11).

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Acknowledgment

The work was supported by the Russian Foundation for Basic Research (No. 12-04-31183, 12-04-00669-a) and the RAS Program “Molecular and Cellular Biology.”

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Authors and Affiliations

  1. G. B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-East Branch, Russian Academy of Sciences, 690022, Vladivostok, Prosp. 100-Letiya Vladivostoka, 159, Russia

    A. S. Sil′chenko, M. I. Kusaikin, A. M. Zakharenko & T. N. Zvyagintseva

Authors
  1. A. S. Sil′chenko
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  2. M. I. Kusaikin
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  3. A. M. Zakharenko
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  4. T. N. Zvyagintseva
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Corresponding author

Correspondence to M. I. Kusaikin.

Additional information

Translated from Khimiya Prirodnykh Soedinenii, No. 2, March–April, 2013, pp. 188–190.

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Sil′chenko, A.S., Kusaikin, M.I., Zakharenko, A.M. et al. Isolation from the marine mollusk Lambis sp. and catalytic properties of an alginate lyase with rare substrate specificity. Chem Nat Compd 49, 215–218 (2013). https://doi.org/10.1007/s10600-013-0564-6

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  • DOI: https://doi.org/10.1007/s10600-013-0564-6

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