Novel thermostable endo-xylanase cloned and expressed from bacterium Geobacillus sp. WSUCF1

• Published in: Bioresource technology Vol. 165; pp. 314 - 318
• Main Authors: Bhalla, Aditya, Bischoff, Kenneth M., Uppugundla, Nirmal, Balan, Venkatesh, Sani, Rajesh K.
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Kidlington Elsevier Ltd 01.08.2014; Elsevier
• Subjects: AFEX-treated corn stover; Agronomy. Soil science and plant productions; Avena - metabolism; Base Sequence; Betula - metabolism; Biofuel production; Biofuels; Biological and medical sciences; Biotechnology; Cloning, Molecular; Conversion; Corn; Electrophoresis, Polyacrylamide Gel; Endo-1,4-beta Xylanases - metabolism; Endo-xylanase; Energy; Enzyme Stability; Enzymes; Escherichia coli; Food industries; Fundamental and applied biological sciences. Psychology; Fungi - enzymology; General agronomy. Plant production; Geobacillus - enzymology; Hydrolysis; Industrial applications and implications. Economical aspects; Lignin - metabolism; Lignocellulose; Optimization; Phylogeny; Recombinant; Recombinant Proteins - metabolism; Temperature; Thermostable; Use and upgrading of agricultural and food by-products. Biotechnology; Use of agricultural and forest wastes. Biomass use, bioconversion; Xylans - metabolism; Thermostable; AFEX-treated corn stover; Endo-xylanase; Biofuels; Monocotyledones; Zea mays; Enzyme; Biofuel; Cereal crop; Xylanolytic enzyme; Straw; Gramineae; Angiospermae; Bacteria; Spermatophyta; Corn by product
• ISSN: 0960-8524; 1873-2976
• DOI: 10.1016/j.biortech.2014.03.112

•A gene encoding a GH10 endo-xylanase from Geobacillus sp. WSUCF1 was cloned and overexpressed.•Endo-xylanase exhibited high specific activity, activity at higher pHs and wide substrate specificity.•Endo-xylanase released high levels of industrially important xylo-oligosaccharides from xylan.•Better lignocellulose conversions to sugars were obtained compared to commercial endo-xylanase. A gene encoding a GH10 endo-xylanase from Geobacillus sp. WSUCF1 was cloned and expressed in Escherichia coli. Recombinant endo-xylanase (37kDa) exhibited high specific activity of 461.0U/mg of protein. Endo-xylanase was optimally active on birchwood xylan at 70°C and pH 6.5. The endo-xylanase was found to be highly thermostable at 50 and 60°C, retaining 82% and 50% of its original activity, respectively, after 60h. High xylan conversions (92%) were obtained with oat-spelt xylan hydrolysis. Higher glucan and xylan conversions were obtained on AFEX-treated corn stover with an enzyme cocktail containing WSUCF1 endo-xylanase (71% and 47%) as compared to enzyme cocktail containing commercial fungal endo-xylanase (64% and 41%). High specific activity, active at high pH’s, wide substrate specificity, and higher hydrolytic activity on recalcitrant lignocellulose, make this endo-xylanase a suitable candidate for biofuel and bioprocess industries.