Multi-Functional Alginate Lyase AlgVR7 from Vibrio rumoiensis: Structural Insights and Catalytic Mechanisms DOI Creative Commons
Zhe Huang, Shuai Liang, Wenhui Jiang

et al.

Marine Drugs, Journal Year: 2025, Volume and Issue: 23(3), P. 124 - 124

Published: March 13, 2025

In this study, we identified AlgVR7, a novel bifunctional alginate lyase from Vibrio rumoiensis and characterized its biochemical properties substrate specificity. Sequence alignment analysis inferred the key residues K267, H162, N86, E189, T244 for AlgVR7 catalysis, it is derived PL7 family; exhibited high activity towards sodium alginate, polyM (PM), polyG (PG); can also degrade polygalacturonic acid (PGA) efficiently, with highest affinity catalytic efficiency MG block of substrate. The optimal temperature pH were determined to be 40 °C 8, respectively. enzyme was maximum at °C, 40% retained after incubation 60 min, still present min incubation. stimulated by 100 Mm NaCl, indicating halophilic nature suitability marine environments. Degradation products analyzed using ESI-MS revealed that primarily produced trisaccharides tetrasaccharides. At 8.0, Km values PM, PG 16.67 μmol, 13.12 22.86 Structural molecular docking studies unveiled involved in recognition interaction. Glu167 as critical residue PL7_5 subfamily, uniquely playing an essential role decomposition. Overall, exhibits great potential powerful efficient preparation oligosaccharides, promising applications biotechnology industrial fields.

Language: Английский

Identification and characterization of a critical loop for the high activity of alginate lyase VaAly2 from the PL7_5 subfamily DOI Creative Commons

Muxuan Du,

Xue Li, Weipeng Qi

et al.

Frontiers in Microbiology, Journal Year: 2024, Volume and Issue: 14

Published: Jan. 12, 2024

As the major component in cell wall of brown algae, alginates are degradable by alginate lyases via β-elimination. Alginate can be categorized into various polysaccharide lyase (PL) families, and PL7 family largest group divided six subfamilies. However, difference among different subfamilies is not fully understood. In this work, a marine lyase, VaAly2, from Vibrio alginolyticus ATCC 17749 belonging to PL7_5 subfamily was identified characterized. It displayed comparatively high alginolytic activities toward substrates functions as bifunctional lyase. Molecular docking biochemical analysis suggested that VaAly2 only contains key catalyzing motif (HQY) conserved but also exhibits some specific characters limited members, such residues long loop1 structure around active center. Our work provides insight loop center site which plays an important role activity substrate binding subfamily.

Language: Английский

Citations

4
Development and characterization of potential antibacterial biocomposites: lysozyme-loaded cellulose-alginate materials DOI

Carlos Eduardo Camacho-González,

Alejandro Pérez-Larios, César Salvador Cardona‐Félix

et al.

Colloids and Surfaces B Biointerfaces, Journal Year: 2025, Volume and Issue: unknown, P. 114536 - 114536

Published: Jan. 1, 2025

Language: Английский

Citations

0
Insights into the mechanism of substrate specificity in a novel PL15_3 subfamily oligo-alginate lyase VBAly15A DOI Creative Commons

Y.T. Tang,

Ziyan Song,

Xiaodong Xu

et al.

Applied and Environmental Microbiology, Journal Year: 2025, Volume and Issue: unknown

Published: Feb. 27, 2025

ABSTRACT Alginate is a major component of brown algae cell walls and can be degraded via β-elimination by alginate lyases. These enzymes are classified into polysaccharide lyases oligo-alginate (Oals), with Oals mainly represented the PL15 PL17 families. Unlike Oals, which widely present in alginate-degrading microorganisms, only identified limited number their biochemical characteristics remain poorly understood. In this research, novel lyase, VBAly15A, from marine bacterium, Vibrio sp. B1Z05, was characterized. It belongs to new PL15_3 subfamily exhibits high activity toward polyM substrates. VBAly15A thermostable medium temperatures, tolerant alkaline up 11.0, polyM-specific Oal, it first degrade polymers disaccharides subsequently catalyze monomers an exolytic mode. Site-directed mutagenesis showed that Arg 114 , Tyr 470 110 active groove essential for stable binding substrate. addition, amino acid His 226 previously suggested act as catalytic base, not catalysis, whereas 280 proposed acid, required enzyme activity. Structural bioinformatic analyses revealed functions specifically abstracting protons G-type substrates, while acts both base. This mechanism likely conserved family IMPORTANCE Alginate, renewable resource sustainability, has great application prospects. addition lyases, critical full degradation alginate, key prerequisite biorefinery. So far, most well-characterized belong family. However, limited, even base fully elucidated. The significance study lies discovering characterizing Oal divides subfamily, PL15_3. Not residues involved identified, but acting also demonstrated. distance C5 proton sugar ring determines substrate specificity. Therefore, work provides insights specificity

Language: Английский

Citations

0
Insights into putative alginate lyases from epipelagic and mesopelagic communities of the global ocean DOI Creative Commons
Mariana Lozada, Hebe M. Dionisi

Scientific Reports, Journal Year: 2025, Volume and Issue: 15(1)

Published: March 8, 2025

Alginate lyases and oligoalginate catalyze the cleavage of glycosidic bonds alginate, an acidic polysaccharide synthesized by brown algae other organisms. These enzymes are highly diverse, currently classified into 15 families Carbohydrate-Active Enzyme (CAZy) database. We explored structural taxonomic diversity, biogeographic distribution genes transcripts, potential environmental drivers putative alginate-degrading from picoplanktonic communities upper layers global ocean. The identified sequences were first analyzed using sequence similarity networks to assess their relationship with CAZy members. Sequences related PL5, PL6, PL7, PL17, PL38 had higher gene transcript abundances, temperature being a key driver structuring community members carrying alginate lyase genes. PL5 homologs included variants in residue active site, assigned 'Candidatus Pelagibacter' showed high abundances that negatively correlated inorganic phosphorus concentrations. Flavobacteriia and/or Gammaproteobacteria classes dominated PL17 families, particular those closely uncultured Polaribacter Alteromonas australica. In family, while taxa Planctomycetota, Verrucomicrobiota, Bacteroidota phyla highest relative abundance at most regions depths, expression levels observed latitudes Eukaryota (e.g., Phaeocystis antarctica). Overall, uncovered this study could be involved various physiological processes, including assimilation biosynthesis.

Language: Английский

Citations

0
Multi-Functional Alginate Lyase AlgVR7 from Vibrio rumoiensis: Structural Insights and Catalytic Mechanisms DOI Creative Commons
Zhe Huang, Shuai Liang, Wenhui Jiang

et al.

Marine Drugs, Journal Year: 2025, Volume and Issue: 23(3), P. 124 - 124

Published: March 13, 2025

In this study, we identified AlgVR7, a novel bifunctional alginate lyase from Vibrio rumoiensis and characterized its biochemical properties substrate specificity. Sequence alignment analysis inferred the key residues K267, H162, N86, E189, T244 for AlgVR7 catalysis, it is derived PL7 family; exhibited high activity towards sodium alginate, polyM (PM), polyG (PG); can also degrade polygalacturonic acid (PGA) efficiently, with highest affinity catalytic efficiency MG block of substrate. The optimal temperature pH were determined to be 40 °C 8, respectively. enzyme was maximum at °C, 40% retained after incubation 60 min, still present min incubation. stimulated by 100 Mm NaCl, indicating halophilic nature suitability marine environments. Degradation products analyzed using ESI-MS revealed that primarily produced trisaccharides tetrasaccharides. At 8.0, Km values PM, PG 16.67 μmol, 13.12 22.86 Structural molecular docking studies unveiled involved in recognition interaction. Glu167 as critical residue PL7_5 subfamily, uniquely playing an essential role decomposition. Overall, exhibits great potential powerful efficient preparation oligosaccharides, promising applications biotechnology industrial fields.

Language: Английский

Citations

0