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Received August 11, 2014
Accepted September 21, 2014
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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
Department of Chemical Engineering, Kyung Hee University, Gyeonggy 446-701, Korea 1Department of Food Science and Biotechnology, Kyungsung University, Busan 608-736, Korea
Korean Journal of Chemical Engineering, May 2015, 32(5), 917-924(8), 10.1007/s11814-014-0282-1
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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 oC. 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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References
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Kam N, Park YJ, Lee EY, Kim HS, Can. J. Microbiol., 57, 1032 (2011)
Kawamoto H, Horibe A, Miki Y, Kimura T, Tanaka K, Nakagawa T, Kawamukai M, Matsuda H, Mar. Biotechnol., 8, 481 (2006)
Kim DE, Lee EY, Kim HS, Mar. Biotechnol., 11, 10 (2009)
Lee SI, Choi SH, Lee EY, Kim HS, Appl. Microbiol. Biotechnol., 95(6), 1643 (2012)
Rahman MM, Inoue A, Tanaka H, Ojima T, Comp. Biochem. Phys. B, 157, 317 (2010)
Pecina A, Pascual A, Paneque A, J. Bacteriol., 181, 1409 (1999)
Gimmestad M, Ertesvag H, Heggeset TMB, Aarstad O, Svanem BIG, Valla S, J. Bacteriol., 191, 4845 (2009)
Hashimoto W, Miyake O, Momma K, Kawai S, Murata K, J. Bacteriol., 182, 4572 (2000)
Ochiai A, Hashimoto W, Murata K, Res. Microbiol., 157, 642 (2006)
Ochiai A, Yamasaki M, Mikami B, Hashimoto W, Murata K, J. Biol. Chem., 285, 24519 (2010)
Park HH, Kam N, Lee EY, Kim HS, Mar. Biotechnol., 14, 189 (2012)
Suzuki H, Suzuki K, Inoue A, Ojima T, Carbohydr. Res., 341, 1809 (2006)
Ryu M, Lee EY, J. Ind. Eng. Chem., 17(5-6), 853 (2011)
Shin JW, Choi SH, Kim DE, Kim HS, Lee JW, Lee IS, Lee EY, Biopro. Biosyst. Eng., 34, 113 (2011)
Hernandez-Carmona G, McHugh DJ, Arvizu-Higuera DL, Rodriguez-Montesinos YE, J. Appl. Phycol., 10, 507 (1999)
Wargacki AJ, Leonard E, Win MN, Regitsky DD, Santos CNS, Kim PB, Cooper SR, Raisner RM, Herman A, Sivitz AB, Lakshmanaswamy A, Kashiyama Y, Baker D, Yoshikuni Y, Science, 335(6066), 308 (2012)
Haug A, Larsen B, Smidsrot O, Acta. Chem. Scand., 20, 183 (1966)
Warren L, Nature, 186, 237 (1960)
Shaya D, Tocilj A, Li Y, Myette J, Venkataraman G, Sasisekhara R, Cygler M, J. Biol. Chem., 281, 15525 (2006)
