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Molecular characterization of a novel oligoalginate lyase consisting of AlgL- and heparinase II/III-like domains from Stenotrophomonas maltophilia KJ-2 and its application to alginate saccharification

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Abstract

Molecular identification and development of a novel recombinant alginate lyase as the biocatalyst for alginate saccharification are prerequisite for bioethanol fermentation from brown seaweed biomass. We identified and characterized a novel oligoalginate lyase for complete degradation of alginate from Stenotrophomonas maltophilia KJ-2 that grow on alginate as the sole carbon source. KJ-2 oligoalginate lyase consisted of AlgL- and heparinase II/III-like domains. The recombinant KJ-2 oligoalginate lyase exhibited substrate preference toward polymannuronate and alginate as well as oligoalginate. The recombinant KJ-2 oligoalginate lyase completely degraded alginate into unsaturated uronate monomer most efficiently at pH 7.5 and 37 °C. Interestingly, AlgL-like recombinant proteins showed more like endolytic activity. The recombinant KJ-2 oligoalginate lyase was a novel oligoalginate lyase consisting of AlgL- and heparinase-like domains and could be used as a candidate for biocatalyst selection to saccharify alginate for bioethanol production from brown seaweed.

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Authors and Affiliations

  1. Department of Chemical Engineering, Kyung Hee University, Gyeonggy, 446-701, Korea

    Jung Won Shin, Ok Kyung Lee & Eun Yeol Lee

  2. Department of Food Science and Biotechnology, Kyungsung University, Busan, 608-736, Korea

    Hwan Hee Park & Hee Sook Kim

Authors
  1. Jung Won Shin
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  2. Ok Kyung Lee
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  3. Hwan Hee Park
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  4. Hee Sook Kim
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  5. Eun Yeol Lee
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Corresponding author

Correspondence to Eun Yeol Lee.

Additional information

This article is dedicated to Prof. Hwayong Kim on the occasion of his retirement from Seoul National Univerisity.

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Shin, J.W., Lee, O.K., Park, H.H. et al. Molecular characterization of a novel oligoalginate lyase consisting of AlgL- and heparinase II/III-like domains from Stenotrophomonas maltophilia KJ-2 and its application to alginate saccharification. Korean J. Chem. Eng. 32, 917–924 (2015). https://doi.org/10.1007/s11814-014-0282-1

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  • DOI: https://doi.org/10.1007/s11814-014-0282-1

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