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 Km, Vmax, and kcat of Bgl1973 were 0.22 mM, 44.44 μmol/min mg, and 57.78 s−1, respectively. Bgl1973 had a high specific activity for pNPGlc (19.10 ± 0.59 U/mg) and salicin (20.43 ± 0.92 U/mg). Furthermore, molecular docking indicated that the glucose binding location and the narrow and deep active channel geometry might contribute to the glucose tolerance of Bgl1973. Our results lay a foundation for the studying of this glucose-tolerant β-glucosidase and its applications in many industrial settings.
Key points
• A novel β-glucosidase from GH3 was obtained from Leifsonia sp. ZF2019.
• Bgl1973 demonstrated excellent glucose tolerance.
• The glucose tolerance of Bgl1973 was explained using molecular docking analysis.
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Acknowledgements
We thank Dr. David Waugh (National Cancer Institute) for the generous gift of the protein expression vector pET28-HMT and the TEV protease expression strain. In addition, we also thank LetPub (www.letpub.com) for its linguistic assistance during the preparation of this manuscript.
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This work was supported by the National Natural Science Foundation of China (31970042) and Zhejiang Provincial Natural Science Foundation of China (LY17C200019).
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Y.H. and G.Z.X. contributed to the conception and design of this study and the interpretation of data; Y.H., C.X.W., and R.H.J. performed experiments; Y.H., Q.X.N, Y.W., Q.X.G, and Y.Z.Z. analyzed the data; Y.H. and G.Z.X. wrote the manuscript. All authors contributed to critical revision of the manuscript and gave final approval of the manuscript for publication.
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He, Y., Wang, C., Jiao, R. et al. Biochemical characterization of a novel glucose-tolerant GH3 β-glucosidase (Bgl1973) from Leifsonia sp. ZF2019. Appl Microbiol Biotechnol 106, 5063–5079 (2022). https://doi.org/10.1007/s00253-022-12064-0
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DOI: https://doi.org/10.1007/s00253-022-12064-0