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Heterologous production and biochemical characterization of a new highly glucose tolerant GH1 β-glucosidase from Anoxybacillus thermarum

AuthorsZaghetto de Almeida, Paula; Oliveira, Tássio Brito de; Coutinho de Lucas, Rosymar; Santos Salgado, Jose Carlos; Martínez Pérez, Malena; Galán, Beatriz ; García, José Luis ; Teixeira de Moraes Polizeli, Maria de Lourdes
Anoxybacillus thermarum
Glucose tolerance
Xylose tolerance
Issue DateDec-2020
CitationProcess Biochemistry 99: 1-8 (2020)
AbstractThe enzymatic lignocellulosic biomass conversion into value-added products requires the use of enzyme-rich cocktails, including β-glucosidases that hydrolyze cellobiose and cellooligosaccharides to glucose. During hydrolysis occurs accumulation of monomers causing inhibition of some enzymes; thus, glucose/xylose tolerant β-glucosidases could overcome this drawback. The search of new tolerant enzymes showing additional properties,such as high activity, wide-pH range, and thermal stability is very relevant to improve the bioprocess. We describe a novel β-glucosidase GH1 from the thermophilic Anoxybacillus thermarum (BgAt), which stood out by the robustness combination of great glucose/xylose tolerance, thermal stability, and high Vmax. The recombinant his-tagged-BgAt was overexpressed in Escherichia coli, was purified in one step, showed a high glucose/xylose tolerance, and activity stimulation (presence of 0.4M glucose/1.0M xylose). The optimal activity was at 65 °C - pH 7.0. BgAt presented an extraordinary temperature stability (48 h – 50 °C), and pH stability (5.5–8.0). The novel enzyme showed outstanding Vmax values compared to other β-glucosidases. Using p-nitrophenyl-β-D-glucopyranoside as substrate the values were Vmax (7614 U/mg), and KM (0.360 mM). These values suffer a displacement in Vmax to 14,026 U/mg (glucose), 14,886 U/mg (xylose), and KM 0.877mM (glucose), and 1.410mM (xylose).
Publisher version (URL)https://doi.org/10.1016/j.procbio.2020.08.013
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