The Identification and Characterization of a Novel Alginate Lyase from Mesonia hitae R32 Exhibiting High Thermal Stability and Potent Antioxidant Oligosaccharide Production DOI Creative Commons

Yongshang Ye,

Zhiyu Li, Ying Zhou

et al.

Marine Drugs, Journal Year: 2025, Volume and Issue: 23(4), P. 176 - 176

Published: April 17, 2025

Alginate lyases are of great importance in biotechnological and industrial processes, yet research on these enzymes from Mesonia genus bacteria is still limited. In this study, a novel PL6 family alginate lyase, MhAly6, was cloned characterized the deep-sea bacterium hitae R32. The enzyme, composed 797 amino acids, contains both GH28 catalytic domains. A phylogenetic analysis revealed its classification into subfamily 1 family. MhAly6 showed optimal activity at 45 °C pH 9.0, retaining over 50% after 210 min incubation 40 °C, highlighting remarkable thermal stability. enzyme exhibited degradation toward sodium alginate, Poly M, G, with highest affinity for natural substrate, producing oligosaccharides (AOSs) degrees polymerization (DP) ranging 2 to 7. Molecular docking identified conserved sites (Lys241/Arg262) Ca2+ binding (Asn202/Glu234/Glu236), while linker domain played an auxiliary role substrate binding. Antioxidant assays that MhAly6-derived AOSs potent radical-scavenging activity, achieving 80.64% 95.39% inhibition rates against DPPH ABTS radicals, respectively. This work not only expands our understanding but also highlights their potential functional antioxidant properties, opening new avenues applications food pharmaceuticals.

Language: Английский

The Identification and Characterization of a Novel Alginate Lyase from Mesonia hitae R32 Exhibiting High Thermal Stability and Potent Antioxidant Oligosaccharide Production DOI Creative Commons

Yongshang Ye,

Zhiyu Li, Ying Zhou

et al.

Marine Drugs, Journal Year: 2025, Volume and Issue: 23(4), P. 176 - 176

Published: April 17, 2025

Alginate lyases are of great importance in biotechnological and industrial processes, yet research on these enzymes from Mesonia genus bacteria is still limited. In this study, a novel PL6 family alginate lyase, MhAly6, was cloned characterized the deep-sea bacterium hitae R32. The enzyme, composed 797 amino acids, contains both GH28 catalytic domains. A phylogenetic analysis revealed its classification into subfamily 1 family. MhAly6 showed optimal activity at 45 °C pH 9.0, retaining over 50% after 210 min incubation 40 °C, highlighting remarkable thermal stability. enzyme exhibited degradation toward sodium alginate, Poly M, G, with highest affinity for natural substrate, producing oligosaccharides (AOSs) degrees polymerization (DP) ranging 2 to 7. Molecular docking identified conserved sites (Lys241/Arg262) Ca2+ binding (Asn202/Glu234/Glu236), while linker domain played an auxiliary role substrate binding. Antioxidant assays that MhAly6-derived AOSs potent radical-scavenging activity, achieving 80.64% 95.39% inhibition rates against DPPH ABTS radicals, respectively. This work not only expands our understanding but also highlights their potential functional antioxidant properties, opening new avenues applications food pharmaceuticals.

Language: Английский

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