Heterologous expression and characterization of xylose-tolerant GH 43 family β-xylosidase/α-L-arabinofuranosidase from Limosilactobacillus fermentum and its application in xylan degradation DOI Creative Commons
Robie Vasquez, Ji Hoon Song, Jae Seung Lee

et al.

Frontiers in Bioengineering and Biotechnology, Journal Year: 2025, Volume and Issue: 13

Published: March 10, 2025

The degradation of hemicellulose, including xylan, is an important industrial process as it provides cheap and sustainable source economically valuable monosaccharides. β-xylosidases are key enzymes required for complete xylan used in the production monosaccharides, such xylose. In this study, we characterized a novel, xylose-tolerant β-xylosidase isolated from Limosilactobacillus fermentum SK152. Sequence analysis protein structure prediction revealed that putative belongs to glycoside hydrolase (GH) family 43 subfamily 11 exhibits high homology with other characterised GH43 fungal bacterial sources. was named Lf Xyl43. catalytic residues Xyl43, which highly conserved among GH β-xylosidases, were predicted. To fully characterise gene encoding heterologously expressed Escherichia coli . Biochemical characterisation recombinant Xyl43 (r Xyl43) active against artificial natural substrates containing β-1,4-xylanopyranosyl residues, p -nitrophenyl-β-D-xylopyranoside (pNPX) oNPX. Moreover, demonstrated weak α-L-arabinofuranosidase activity. optimal activity r obtained at pH 7.0 35°C. could degrade xylo-oligosaccharides, xylobiose, xylotriose, xylotetraose, showed hydrolysing towards beechwood xylan. synergy commercial xylanase degrading rye wheat arabinoxylan. not affected by addition metal ions, chemical reagents, or concentrations NaCl. Notably, exhibited tolerance xylose concentrations, K i value 100.1, comparable β-xylosidases. our knowledge, first identified lactic acid bacterium salt Overall, great potential novel use lignocellulosic material, especially hemicellulose. Its mild conditions, makes suitable enzyme applications.

Language: Английский

Heterologous expression and characterization of xylose-tolerant GH 43 family β-xylosidase/α-L-arabinofuranosidase from Limosilactobacillus fermentum and its application in xylan degradation DOI Creative Commons
Robie Vasquez, Ji Hoon Song, Jae Seung Lee

et al.

Frontiers in Bioengineering and Biotechnology, Journal Year: 2025, Volume and Issue: 13

Published: March 10, 2025

The degradation of hemicellulose, including xylan, is an important industrial process as it provides cheap and sustainable source economically valuable monosaccharides. β-xylosidases are key enzymes required for complete xylan used in the production monosaccharides, such xylose. In this study, we characterized a novel, xylose-tolerant β-xylosidase isolated from Limosilactobacillus fermentum SK152. Sequence analysis protein structure prediction revealed that putative belongs to glycoside hydrolase (GH) family 43 subfamily 11 exhibits high homology with other characterised GH43 fungal bacterial sources. was named Lf Xyl43. catalytic residues Xyl43, which highly conserved among GH β-xylosidases, were predicted. To fully characterise gene encoding heterologously expressed Escherichia coli . Biochemical characterisation recombinant Xyl43 (r Xyl43) active against artificial natural substrates containing β-1,4-xylanopyranosyl residues, p -nitrophenyl-β-D-xylopyranoside (pNPX) oNPX. Moreover, demonstrated weak α-L-arabinofuranosidase activity. optimal activity r obtained at pH 7.0 35°C. could degrade xylo-oligosaccharides, xylobiose, xylotriose, xylotetraose, showed hydrolysing towards beechwood xylan. synergy commercial xylanase degrading rye wheat arabinoxylan. not affected by addition metal ions, chemical reagents, or concentrations NaCl. Notably, exhibited tolerance xylose concentrations, K i value 100.1, comparable β-xylosidases. our knowledge, first identified lactic acid bacterium salt Overall, great potential novel use lignocellulosic material, especially hemicellulose. Its mild conditions, makes suitable enzyme applications.

Language: Английский

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