Utilize este identificador para referenciar este registo: https://hdl.handle.net/10216/154875
Autor(es): Nguyen, TNT
Chataway, T
Araujo, R
Puri, M
Franco, CMM
Título: Purification and characterization of a novel alginate lyase from a marine streptomyces species isolated from seaweed
Editor: MDPI
Data de publicação: 2021
Resumo: Alginate, a natural polysaccharide derived from brown seaweed, is finding multiple applications in biomedicine via its transformation through chemical, physical, and, increasingly, enzymatic processes. In this study a novel alginate lyase, AlyDS44, was purified and characterized from a marine actinobacterium, Streptomyces luridiscabiei, which was isolated from decomposing seaweed. The purified enzyme had a specific activity of 108.6 U/mg, with a molecular weight of 28.6 kDa, and was composed of 260 amino acid residues. AlyDS44 is a bifunctional alginate lyase, active on both polyguluronate and polymannuronate, though it preferentially degrades polyguluronate. The optimal pH of this enzyme is 8.5 and the optimal temperature is 45¿C. It is a salt-tolerant alginate lyase with an optimal activity at 0.6 M NaCl. Metal ions Mn2+, Co2+, and Fe2+ increased the alginate degrading activity, but it was inhibited in the presence of Zn2+ and Cu2+. The highly conserved regions of its amino acid sequences indicated that AlyDS44 belongs to the polysaccharide lyase family 7. The main breakdown products of the enzyme on alginate were disaccharides, trisaccharides, and tetrasaccharides, which demonstrated that this enzyme acted as an endo-type alginate lyase. AlyDS44 is a novel enzyme, with the potential for efficient production of alginate oligosaccharides with low degrees of polymerization.
Assunto: Actinobacteria
Alginate lyase
Bifunctional enzyme
Polysaccharide-degrading enzyme
Protein sequence
URI: https://hdl.handle.net/10216/154875
Fonte: Marine Drugs, vol.19(11):590
Tipo de Documento: Artigo em Revista Científica Internacional
Condições de Acesso: openAccess
Licença: https://creativecommons.org/licenses/by/4.0/
Aparece nas coleções:I3S - Artigo em Revista Científica Internacional

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