Identification and characterization of a novel thermostable PL7 alginate lyase from a submarine volcanic metagenomic library.

Autor: Tsopanakis V; Department of Chemistry, University of Crete, Voutes University Campus, Heraklion 70013, Greece., Anastasiadou E; Department of Chemistry, University of Crete, Voutes University Campus, Heraklion 70013, Greece., Mikkelsen MD; Protein Chemistry and Enzyme Technology Section, Department of Biotechnology and Biomedicine, Technical University of Denmark, Lyngby DK-2800 Kgs, Denmark., Meyer AS; Protein Chemistry and Enzyme Technology Section, Department of Biotechnology and Biomedicine, Technical University of Denmark, Lyngby DK-2800 Kgs, Denmark., Pavlidis IV; Department of Chemistry, University of Crete, Voutes University Campus, Heraklion 70013, Greece. Electronic address: ipavlidis@uoc.gr.
Jazyk: angličtina
Zdroj: Enzyme and microbial technology [Enzyme Microb Technol] 2024 Oct; Vol. 180, pp. 110486. Date of Electronic Publication: 2024 Jul 21.
DOI: 10.1016/j.enzmictec.2024.110486
Abstrakt: 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 58 % 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 ± 8 U/mg) and high thermostability (half-life time of 30 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 440 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.
Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024. Published by Elsevier Inc.)
Databáze: MEDLINE
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