Bi-functional fusion enzyme EG-M-Xyn displaying endoglucanase and xylanase activities and its utility in improving lignocellulose degradation.
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Abstract |
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In this study, the gene fusion of endoglucanase (EG, one of cellulases) from Teleogryllus emma and xylanase (Xyn, one of hemicellulases) from Thermomyces lanuginosus was constructed to generate a fusion enzyme (EG-M-Xyn). Through the expression and purification by ultrafiltration and size-exclusion chromatography, the purified EG-M-Xyn had a molecular weight of 75.5 kDa and exhibited the specific activity of CMCase and xylanase as 306.8 U/mg and 1227.3 U/mg, respectively. The Km values (CMC and beechwood xylan) were 6.8 and 60.6 mg mL-1 while catalytic efficiency (kcat/Km) values of CMCase and xylanase were 3280 and 38,797 min-1 mg-1 mL, respectively. EG-M-Xyn exerted great properties for its great potential in improving the enzymatic hydrolysis of lignocellulosics to produce fermentable sugars. First, EG-M-Xyn showed mild reaction pH and temperature of 5.5 and 50 °C, respectively. Secondly, EG-M-Xyn exhibited great heat tolerance of T1/2 values of 173 (CMCase) and 693 min (xylanase). Lastly and most importantly, application of EG-M-Xyn in combination with Ctec2 (commercial enzyme) in the saccharification led to a 10-20% net increase in fermentable sugars liberated from pretreated rice straw in comparison to the Ctec2 alone group. In conclusion, EG-M-Xyn had great potential in generating fermentable sugars from renewable agro-residues for biofuel and fine chemical industry. |
Year of Publication |
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2018
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Journal |
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International journal of biological macromolecules
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Date Published |
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2018
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ISSN Number |
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0141-8130
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URL |
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http://linkinghub.elsevier.com/retrieve/pii/S0141-8130(17)34796-7
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DOI |
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10.1016/j.ijbiomac.2018.01.080
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Short Title |
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Int J Biol Macromol
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