AI Article Synopsis
- A new β-glucosidase gene named unbgl1A was identified from a metagenomic library, expressed in E. coli, and characterized biochemically, demonstrating optimal activity at pH 6.0 and 50°C.
- The enzyme has a Km of 2.09 mM and a Vmax of 183.90 μmol min(-1) mg(-1), with high stability and activity even in high concentrations of NaCl and glucose (up to 2000 mM).
- Unbgl1A also displays transglucosylation abilities, converting cellobiose to cellotriose, which suggests its potential for industrial applications in glucose and bioethanol production from lignocellulos
Article Abstract
A β-glucosidase gene unbgl1A was isolated by the function-based screening of a metagenomic library and the enzyme protein was expressed in Escherichia coli, purified, and biochemically characterized. The enzyme Unbgl1A had a Km value of 2.09 ± 0.31 mM, and a Vmax value of 183.90 ± 9.61 μmol min(-1) mg(-1) under the optimal reaction conditions, which were pH 6.0 at 50°C. Unbgl1A can be activated by a variety of monosaccharides, disaccharides, and NaCl, and exhibits a high level of stability at high concentration of NaCl. Two prominent features for this enzyme are: (i) high glucose tolerance. It can be tolerant to glucose as high as 2000 mM, with Ki = 1500 mM; (ii) high NaCl tolerance. Its activity is not affected by 600 mM NaCl. The enzyme showed transglucosylation activities resulting in the formation of cellotriose from cellobiose. These properties of Unbgl1A should have important practical implication in its potential applications for better industrial production of glucose or bioethanol started from lignocellulosic biomass.
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