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

и другие.

Marine Drugs, Год журнала: 2025, Номер 23(4), С. 176 - 176

Опубликована: Апрель 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.

Язык: Английский

Smart stimuli-responsive hydrogels for safe oral administration of Insulin: A Review DOI
Nan Jiang,

Xiangjun Yu,

Jing Zhang

и другие.

International Journal of Pharmaceutics, Год журнала: 2025, Номер unknown, С. 125487 - 125487

Опубликована: Март 1, 2025

Язык: Английский

Процитировано

0
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

и другие.

Marine Drugs, Год журнала: 2025, Номер 23(4), С. 176 - 176

Опубликована: Апрель 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.

Язык: Английский

Процитировано

0