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Characterization and Application of an Alginate Lyase, Aly1281 from Marine Bacterium Pseudoalteromonas carrageenovora ASY5.
Zhang, Yong-Hui; Shao, Yuan; Jiao, Chao; Yang, Qiu-Ming; Weng, Hui-Fen; Xiao, An-Feng.
Afiliação
  • Zhang YH; College of Food and Biological Engineering, Jimei University, Xiamen 361021, China.
  • Shao Y; Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Xiamen 361021, China.
  • Jiao C; Xiamen Key Laboratory of Marine Functional Food, Xiamen 361021, China.
  • Yang QM; College of Food and Biological Engineering, Jimei University, Xiamen 361021, China.
  • Weng HF; Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Xiamen 361021, China.
  • Xiao AF; Xiamen Key Laboratory of Marine Functional Food, Xiamen 361021, China.
Mar Drugs ; 18(2)2020 Jan 31.
Article em En | MEDLINE | ID: mdl-32023889
ABSTRACT
Alginate extracted from widely cultured brown seaweed can be hydrolyzed by alginate lyase to produce alginate oligosaccharides (AOS) with intriguing biological activities. Herein, a novel alginate lyase Aly1281 was cloned from marine bacterium Pseudoalteromonas carrageenovora ASY5 isolated from mangrove soil and found to belong to polysaccharide lyase family 7. Aly1281 exhibited maximum activity at pH 8.0 and 50 °C and have broad substrate specificity for polyguluronate and polymannuronate. Compared with other alginate lyases, Aly1281 exhibited high degradation specificity and mainly produced di-alginate oligosaccharides which displayed good antioxidant function to reduce ferric and scavenge radicals such as hydroxyl, ABTS+ and DPPH. Moreover, the catalytic activity and kinetic performance of Aly1281 were highly improved with the addition of salt, demonstrating a salt-activation property. A putative conformational structural feature of Aly1281 was found by MD simulation analysis for understanding the salt-activation effect.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polissacarídeo-Liases / Pseudoalteromonas Idioma: En Revista: Mar Drugs Assunto da revista: BIOLOGIA / FARMACOLOGIA Ano de publicação: 2020 Tipo de documento: Article País de afiliação: China

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polissacarídeo-Liases / Pseudoalteromonas Idioma: En Revista: Mar Drugs Assunto da revista: BIOLOGIA / FARMACOLOGIA Ano de publicação: 2020 Tipo de documento: Article País de afiliação: China