Functional Characterization of a Highly Efficient Endoglucanase from Bacillus licheniformis BJ2022 and Its Application in the Preparation of Low-Molecular-Weight Konjac Glucomannan DOI
Tianxiang Zhu, Songlin Liu, Yu Gao

et al.

Journal of Agricultural and Food Chemistry, Journal Year: 2025, Volume and Issue: unknown

Published: March 26, 2025

Endoglucanases may not only act on β-1,4-linkages in β-glucan but also target d-glucose glucomannan, which can expand their utility the preparation of prebiotics. In this study, a highly efficient endoglucanase (BlGH5) from Bacillus licheniformis BJ2022 was expressed and characterized. BlGH5 exhibited highest activity at pH 7.0 60 °C. It maintained over 80% 4.0-7.0 30-60 specifically cleaved β-1,4-glycosidic bonds linked to d-glucose. Site-directed mutagenesis results suggested that Arg91, Asn167, Glu168, Trp206, His228, Tyr230, Ser263, Trp290 are key residues for its binding catalytic activity. Moreover, displayed high against konjac glucomannan (KGM), indicating could be used prepare low-molecular-weight (KGM-L). Based physicochemical properties KGM KGM-L, KGM-L characterized by reduced molecular weight viscosity. Fecal fermentation experiments demonstrated promote production short-chain fatty acids (SCFAs). Still, more conducive growth gut probiotics. conclusion, we identified an degradation KGM. Results indicated would have superior prebiotic effects. Thus, our study provides basis future development application as prebiotic.

Language: Английский

Functional Characterization of a Highly Efficient Endoglucanase from Bacillus licheniformis BJ2022 and Its Application in the Preparation of Low-Molecular-Weight Konjac Glucomannan DOI
Tianxiang Zhu, Songlin Liu, Yu Gao

et al.

Journal of Agricultural and Food Chemistry, Journal Year: 2025, Volume and Issue: unknown

Published: March 26, 2025

Endoglucanases may not only act on β-1,4-linkages in β-glucan but also target d-glucose glucomannan, which can expand their utility the preparation of prebiotics. In this study, a highly efficient endoglucanase (BlGH5) from Bacillus licheniformis BJ2022 was expressed and characterized. BlGH5 exhibited highest activity at pH 7.0 60 °C. It maintained over 80% 4.0-7.0 30-60 specifically cleaved β-1,4-glycosidic bonds linked to d-glucose. Site-directed mutagenesis results suggested that Arg91, Asn167, Glu168, Trp206, His228, Tyr230, Ser263, Trp290 are key residues for its binding catalytic activity. Moreover, displayed high against konjac glucomannan (KGM), indicating could be used prepare low-molecular-weight (KGM-L). Based physicochemical properties KGM KGM-L, KGM-L characterized by reduced molecular weight viscosity. Fecal fermentation experiments demonstrated promote production short-chain fatty acids (SCFAs). Still, more conducive growth gut probiotics. conclusion, we identified an degradation KGM. Results indicated would have superior prebiotic effects. Thus, our study provides basis future development application as prebiotic.

Language: Английский

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