Identification and characterization of a novel thermostable PL7 alginate lyase from a submarine volcanic metagenomic library.
Enzyme Microb Technol
; 180: 110486, 2024 Jul 21.
Article
en En
| MEDLINE
| ID: mdl-39038418
ABSTRACT
Seaweed biomass is as an abundant and renewable source of complex polysaccharides, including alginate which has a variety of applications. A sustainable method for exploiting alginate towards the production of valuable oligosaccharides is through enzymatic processing, using alginate lyases. Industrial refinement methods demand robust enzymes. Metagenomic libraries from extreme environments are a new source of unique enzymes with great industrial potential. Herein we report the identification of a new thermostable alginate lyase with only 58â¯% identity to known sequences, identified by mining a metagenomic library obtained from the hydrothermal vents of the volcano Kolumbo in the Aegean Sea (Kolumbo Alginate Lyase, KAlLy). Sequence analysis and biochemical characterization of KAlLy showed that this new alginate lyase is a Polysaccharide Lyase of family 7 (PL7) enzyme with endo- and exo-action on alginate and poly-mannuronic acid, with high activity at 60°C (56 ± 8â¯U/mg) and high thermostability (half-life time of 30â¯h at 50°C). The response surface methodology analysis revealed that the reaction optimum conditions with poly-mannuronic acid as substrate are 44°C, pH of 5.5 with 440â¯mM NaCl. This novel alginate lyase is a valuable addition to the toolbox of alginate modifying enzymes, due to its diverse sequence and its good thermal stability.
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Colección:
01-internacional
Base de datos:
MEDLINE
Idioma:
En
Revista:
Enzyme Microb Technol
Año:
2024
Tipo del documento:
Article
Pais de publicación:
Estados Unidos