Characterization of a new alginate lyase from newly isolated <i>Flavobacterium</i> sp. S20

DOI PDF PDF Web Site 被引用文献2件
  • Lishuxin Huang
    grid.9227.e 0000000119573309 Natural Products and Glyco-Biotechnology Research Group, Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics Chinese Academy of Sciences, CAS 116023 Dalian People’s Republic of China
  • Jungang Zhou
    grid.8547.e 0000000101252443 State Key Laboratory of Genetic Engineering Fudan University 200433 Shanghai People’s Republic of China
  • Xiao Li
    grid.412262.1 0000000417615538 Shan Xi Provincial Key Laboratory of Biotechnology, Key Laboratory of Resource Biology and Biotechnology in Western China, Ministry of Education, Life Science College Northwest University 710069 Xi’an People’s Republic of China
  • Qiang Peng
    grid.9227.e 0000000119573309 Natural Products and Glyco-Biotechnology Research Group, Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics Chinese Academy of Sciences, CAS 116023 Dalian People’s Republic of China
  • Hong Lu
    grid.8547.e 0000000101252443 State Key Laboratory of Genetic Engineering Fudan University 200433 Shanghai People’s Republic of China
  • Yuguang Du
    grid.9227.e 0000000119573309 Natural Products and Glyco-Biotechnology Research Group, Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics Chinese Academy of Sciences, CAS 116023 Dalian People’s Republic of China

書誌事項

公開日
2013-01-01
権利情報
  • https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model
DOI
  • 10.1007/s10295-012-1210-1
公開者
Oxford University Press (OUP)

この論文をさがす

説明

<jats:title>Abstract</jats:title> <jats:p>Alginate lyase is a promising biocatalyst because of its application in saccharification of alginate for the production of biochemicals and renewable biofuels. This study described the isolation of a new alginate metabolizing bacterium, Flavobacterium sp. S20, from sludge samples and the characterization of its alginate lyase Alg2A. The alginate lyase gene, alg2A, was obtained by constructing and screening the genomic library of the strain S20 and overexpressed in Escherichia coli. Substrate specificity assays indicated Alg2A preferred poly-α-l-guluronate as a substrate over poly-β-d-mannuronate. In the saccharification process of a high content (10 %, w/v) of sodium alginate, the recombinant alginate lyase Alg2A yielded 152 of mM the reducing sugars after 69 h of reaction, and the amounts of oligosaccharides with a different degree of polymerization (DP) generated by Alg2A gradually accumulated without significant variation in the distribution of oligosaccharide compositions. These results indicated that Alg2A possessed high enzymatic capability for saccharifying the alginate, which could be used in saccharifying the alginate biomass prior to the main fermentation process for biofuels. In addition, Alg2A had a different endolytic reaction mode from both the two commercial alginate lyases and other alginate lyases from polysaccharide lyase family 7 owing to high yields of penta-, hex-, and hepta-saccharides in the hydrolysis products of Alg2A. Thus, Alg2A could be a good tool for the large-scale preparation of alginate oligosaccharides with high DP.</jats:p>

収録刊行物

被引用文献 (2)*注記

もっと見る

問題の指摘

ページトップへ