A β-Galactosidase acting on unique galactosides: the structure and function of a β-1,2-galactosidase fromBacteroides xylanisolvens, an intestinal bacterium DOI Creative Commons

Yutaka Nakazawa,

Masumi Kageyama,

Tomohiko Matsuzawa

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: May 5, 2024

Abstract Galactosides are major carbohydrates that found in plant cell walls and various prebiotic oligosaccharides. Studying the detailed biochemical functions of β-galactosidases degrading these is important. In particular, identifying with new substrate specificities could help production potentially beneficial this study, we identified a β-galactosidase novel specificity from Bacteroides xylanisolvens , an intestinal bacterium. The enzyme did not show hydrolytic activity toward natural β-galactosides during first screening. However, when α-D-galactosyl fluoride (α-GalF) as donor galactose or D-fucose acceptor were incubated nucleophile mutant, reaction products detected. galactobiose produced α-GalF was β-1,2-galactobiose using NMR. Kinetic analysis revealed effectively hydrolyzed β-1,2-galactotriose. complex structure methyl β-galactopyranose ligand, ligand only located at subsite +1. 2-hydroxy group anomeric faces direction −1 solvent, respectively. This observation consistent regarding linkage position chain length. Overall, concluded acting on β-1,2-galactooligosaccharides. Synopsis structural functional bacterium led to discovery hydrolyzing unique

Language: Английский

Structure and function of a β-1,2-galactosidase from Bacteroides xylanisolvens, an intestinal bacterium DOI Creative Commons

Yutaka Nakazawa,

Masumi Kageyama,

Tomohiko Matsuzawa

et al.

Communications Biology, Journal Year: 2025, Volume and Issue: 8(1)

Published: Jan. 16, 2025

Abstract Galactosides are major carbohydrates that found in plant cell walls and various prebiotic oligosaccharides. Studying the detailed biochemical functions of β-galactosidases degrading these is important. In particular, identifying with new substrate specificities could help production potentially beneficial this study, we identify a β-galactosidase novel specificity from Bacteroides xylanisolvens , an intestinal bacterium. The enzyme do not show hydrolytic activity toward natural β-galactosides during first screening. However, when α- d -galactosyl fluoride (α-GalF) as donor galactose or -fucose acceptor incubated nucleophile mutant, reaction products detected. galactobiose produced α-GalF identified β-1,2-galactobiose using NMR. Kinetic analysis reveals effectively hydrolyzes β-1,2-galactotriose. complex structure methyl β-galactopyranose ligand, ligand only located at subsite +1. 2-hydroxy group anomeric faces direction −1 solvent, respectively. This observation consistent regarding linkage position chain length. Overall, conclude acting on β-1,2-galactooligosaccharides.

Language: Английский

Citations

0
Two novel β-galactosidases from Aeromonas caviae with potential industrial applications in milk and catalytic mechanism analysis using molecular docking DOI
Yongmei Lyu,

Fengxiang Chen,

Wanjie Mao

et al.

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 141188 - 141188

Published: Feb. 1, 2025

Language: Английский

Citations

0
Natronomicrosphaera hydrolytica, gen. Nov., sp. nov., a first representative of the phylum Planctomycetota from soda lakes DOI Creative Commons
Dimitry Y. Sorokin, Alexander Y. Merkel, Nicole J. Bale

et al.

Systematic and Applied Microbiology, Journal Year: 2025, Volume and Issue: 48(3), P. 126608 - 126608

Published: April 28, 2025

Language: Английский

Citations

0
A β-Galactosidase acting on unique galactosides: the structure and function of a β-1,2-galactosidase fromBacteroides xylanisolvens, an intestinal bacterium DOI Creative Commons

Yutaka Nakazawa,

Masumi Kageyama,

Tomohiko Matsuzawa

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: May 5, 2024

Abstract Galactosides are major carbohydrates that found in plant cell walls and various prebiotic oligosaccharides. Studying the detailed biochemical functions of β-galactosidases degrading these is important. In particular, identifying with new substrate specificities could help production potentially beneficial this study, we identified a β-galactosidase novel specificity from Bacteroides xylanisolvens , an intestinal bacterium. The enzyme did not show hydrolytic activity toward natural β-galactosides during first screening. However, when α-D-galactosyl fluoride (α-GalF) as donor galactose or D-fucose acceptor were incubated nucleophile mutant, reaction products detected. galactobiose produced α-GalF was β-1,2-galactobiose using NMR. Kinetic analysis revealed effectively hydrolyzed β-1,2-galactotriose. complex structure methyl β-galactopyranose ligand, ligand only located at subsite +1. 2-hydroxy group anomeric faces direction −1 solvent, respectively. This observation consistent regarding linkage position chain length. Overall, concluded acting on β-1,2-galactooligosaccharides. Synopsis structural functional bacterium led to discovery hydrolyzing unique

Language: Английский

Citations

0