The Potential of Using Immobilized Xylanases to Enhance the Hydrolysis of Soluble, Biomass Derived Xylooligomers

Earlier work had indicated that enzyme-mediated hydrolysis of xylooligomer-rich water-soluble streams (derived from steam pre-treated wheat straw) resulted in the effective production of xylose which was subsequently used to produce bio-glycol. In the work reported here, both the thermostability and recyclability of xylanases were significantly improved by covalent immobilizing the enzymes onto alginate beads. The immobilized xylanases showed a lower hydrolytic potential (similar to 55% xylooligomer conversion) compared to the commercial xylanase cocktail HTec3 (similar to 90% xylooligomer conversion) when used at the same protein loading concentration. This was likely due to the less efficient immobilization of key higher molecular weight enzymes (>75 kDa), such as -xylosidases. However, enzyme immobilization could be improved by lowering the glutaraldehyde loading used to activate the alginate beads, resulting in improved hydrolysis efficacy (similar to 65% xylooligomer conversion). Enzyme immobilization improved enzyme thermostability (endoxylanase and -xylosidase activities were improved by 80% and 40%, respectively, after 24 h hydrolysis) and this allowed the immobilized enzymes to be reused/recycled for multiple rounds of hydrolysis (up to five times) without any significant reduction in their hydrolytic potential.