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      Screening of alginate lyase-excreting microorganisms from the surface of brown algae

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          Abstract

          Alginate lyase is a biocatalyst that degrades alginate to produce oligosaccharides, which have many bioactive functions and could be used as renewable biofuels. Here we report a simple and sensitive plate assay for screening alginate lyase-excreting microorganisms from brown algae. Brown algae Laminaria japonica, Sargassum horneri and Sargassum siliquatrum were cultured in sterile water. Bacteria growing on the surface of seaweeds were identified and their capacity of excreting alginate lyase was analyzed. A total of 196 strains were recovered from the three different algae samples and 12 different bacterial strains were identified capable of excreting alginate lyases. Sequence analysis of the 16S rRNA gene revealed that these alginate lyase-excreting strains belong to eight genera: Paenibacillus (4/12), Bacillus (2/12), Leclercia (1/12), Isoptericola (1/12), Planomicrobium (1/12), Pseudomonas (1/12), Lysinibacillus (1/12) and Sphingomonas (1/12). Further analysis showed that the LJ-3 strain ( Bacillus halosaccharovorans) had the highest enzyme activity. To our best knowledge, this is the first report regarding alginate lyase-excreting strains in Paenibacillus, Planomicrobium and Leclercia. We believe that our method used in this study is relatively easy and reliable for large-scale screening of alginate lyase-excreting microorganisms.

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          The online version of this article (doi:10.1186/s13568-017-0361-x) contains supplementary material, which is available to authorized users.

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          Alginates

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            Alginate lyase: Review of major sources and classification, properties, structure-function analysis and applications.

            Alginate lyases catalyze the degradation of alginate, a complex copolymer of α-L-guluronate and its C5 epimer β-D-mannuronate. The enzymes have been isolated from various kinds of organisms with different substrate specificities, including algae, marine mollusks, marine and terrestrial bacteria, and some viruses and fungi. With the progress of structural biology, many kinds of alginate lyases of different polysaccharide lyases families have been characterized by obtaining crystal structures, and the catalytic mechanism has also been elucidated. Combined with various studies, we summarized the source, classification and properties of the alginate lyases from different polysaccharide lyases families. The relationship between substrate specificity and protein sequence was also investigated.
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              Alginate oligosaccharides: enzymatic preparation and antioxidant property evaluation.

              Alginate oligosaccharides (AOs) prepared from alginate, by alginate lyase-mediated depolymerization, were structurally characterized by mass spectrometry, infrared spectrometry and thin layer chromatography. Studies of their antioxidant activities revealed that AOs were able to completely (100%) inhibit lipid oxidation in emulsions, superiorly to ascorbic acid (89% inhibition). AOs showed radical scavenging activity towards ABTṠ, hydroxyl, and superoxide radicals, which might explain their excellent antioxidant activity. The radical scavenging activity is suggested to originate mainly from the presence of the conjugated alkene acid structure formed during enzymatic depolymerization. According to the resonance hybrid theory, the parent radicals of AOs are delocalized through allylic rearrangement, and as a consequence, the reactive intermediates are stabilized. AOs were weak ferrous ion chelators. This work demonstrated that AOs obtained from a facile enzymatic treatment of abundant alginate is an excellent natural antioxidant, which may find applications in the food industry.
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                Author and article information

                Contributors
                wmpdsg@126.com
                stepper95@163.com
                ZZhang@uwyo.edu
                ytwz2006@sina.com
                sqin@yic.ac.cn
                yps6@163.com
                Journal
                AMB Express
                AMB Express
                AMB Express
                Springer Berlin Heidelberg (Berlin/Heidelberg )
                2191-0855
                4 April 2017
                4 April 2017
                2017
                : 7
                : 74
                Affiliations
                [1 ]GRID grid.19373.3f, School of Municipal and Environmental Engineering, , Harbin Institute of Technology, ; Harbin, 150090 China
                [2 ]GRID grid.9227.e, , Yantai Institute of Costal Zone Research Chinese Academy of Sciences, ; 17 Chunhui Road, Yantai, 264003 Shandong province China
                [3 ]GRID grid.135963.b, Department of Zoology and Physiology, , University of Wyoming, ; Laramie, WY USA
                [4 ]Worldfull Agricultural Science and Technology Co., Ltd, Yantai, 264000 China
                [5 ]GRID grid.19373.3f, School of Marine Science and Technology, , Harbin Institute of Technology at Weihai, ; West Culture Road 2, Weihai, 264209 Shandong Province China
                Article
                361
                10.1186/s13568-017-0361-x
                5378567
                28374344
                ea1c7c93-4a49-4b2e-a449-794bada9410e
                © The Author(s) 2017

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

                History
                : 13 January 2017
                : 2 March 2017
                Funding
                Funded by: National Key Technology Research and Development Program of China
                Award ID: 2013BAB01B0
                Award Recipient :
                Funded by: Young Scientists Fund of National Natural Science Foundation of China
                Award ID: 41401285
                Award Recipient :
                Funded by: Public Science and Technology Research Funds Projects of Ocean
                Award ID: 201505022
                Award Recipient :
                Funded by: Chinese Academy of Sciences Strategic Pilot Project
                Award ID: XDA1102040300
                Award Recipient :
                Funded by: Shandong Science and Technology Development Project
                Award ID: 2010GSF10208
                Award Recipient :
                Categories
                Original Article
                Custom metadata
                © The Author(s) 2017

                Biotechnology
                alginate lyase,gram’s iodine,alginate degradation,screening,brown algae
                Biotechnology
                alginate lyase, gram’s iodine, alginate degradation, screening, brown algae

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