ArticleApplied microbiology and biotechnology2022
Biochemical characterization of a novel glucose-tolerant GH3 β-glucosidase (Bgl1973) from Leifsonia sp. ZF2019.
Article in Applied microbiology and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed.
- Characterization, thermostable mechanism, and molecular docking of a novel glucose-tolerantFrontiers in microbiology · 2025Article
- A description of Joostella sp. strain CR20 with potential biotechnological applications.Antonie van Leeuwenhoek · 2024Article
- Phytohormones and related genes function as physiological and molecular switches regulating water stress response in the sunflower.Physiology and molecular biology of plants : an international journal of functional plant biology · 2024Article
- Novel glycosidase from Paenibacillus lactis 154 hydrolyzing the 28-O-β-D-glucopyranosyl ester bond of oleanane-type saponins.Applied microbiology and biotechnology · 2024Article
- A Thermotolerant YeastJournal of fungi (Basel, Switzerland) · 2024Article
- A Recombinant Thermophilic and Glucose-Tolerant GH1 β-Glucosidase Derived from Hehua Hot Spring.Molecules (Basel, Switzerland) · 2024Article
- Characterization of a thermophilic and glucose-tolerant GH1 β-glucosidase from hot springs and its prospective application in corn stover degradation.Frontiers in microbiology · 2023Article
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8 authors.
Funding
Abstract
Beta-glucosidase (Bgl) is an enzyme with considerable food, beverage, and biofuel processing potential. However, as many Bgls are inhibited by their reaction end product glucose, their industrial applications are greatly limited. In this study, a novel Bgl gene (Bgl1973) was cloned from Leifsonia sp. ZF2019 and heterologously expressed in E. coli. Sequence analysis and structure modeling revealed that Bgl1973 was 748 aa, giving it a molecular weight of 78 kDa, and it showed high similarity with the glycoside hydrolase 3 (GH3) family Bgls with which its active site residues were conserved. By using pNPGlc (p-nitrophenyl-β-D-glucopyranoside) as substrate, the optimum temperature and pH of Bgl1973 were shown to be 50 °C and 7.0, respectively. Bgl1973 was insensitive to most metal ions (12.5 mM), 1% urea, and even 0.1% Tween-80. This enzyme maintained 60% of its original activity in the presence of 20% NaCl, demonstrating its excellent salt tolerance. Furthermore, it still had 83% residual activity in 1 M of glucose, displaying its outstanding glucose tolerance. The K
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