Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7077700 | Bioresource Technology | 2014 | 5 Pages |
Abstract
A gene encoding a GH10 endo-xylanase from Geobacillus sp. WSUCF1 was cloned and expressed in Escherichia coli. Recombinant endo-xylanase (37 kDa) exhibited high specific activity of 461.0 U/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 60 h. 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.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Process Chemistry and Technology
Authors
Aditya Bhalla, Kenneth M. Bischoff, Nirmal Uppugundla, Venkatesh Balan, Rajesh K. Sani,