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The Potential of Using Immobilized Xylanases to Enhance the Hydrolysis of Soluble, Biomass Derived Xylooligomers Hu, Jinguang; Davies, Joshua; Mok, Yiu Ki; Arato, Claudio; Saddler, J. N. (John N.), 1953-
Abstract
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 (~55% xylooligomer conversion) compared to the commercial xylanase cocktail HTec3 (~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 β-xylosidases. However, enzyme immobilization could be improved by lowering the glutaraldehyde loading used to activate the alginate beads, resulting in improved hydrolysis efficacy (~65% xylooligomer conversion). Enzyme immobilization improved enzyme thermostability (endoxylanase and β-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.
Item Metadata
Title |
The Potential of Using Immobilized Xylanases to Enhance the Hydrolysis of Soluble, Biomass Derived Xylooligomers
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Creator | |
Publisher |
Multidisciplinary Digital Publishing Institute
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Date Issued |
2018-10-17
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Description |
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 (~55% xylooligomer conversion) compared to the commercial xylanase cocktail HTec3 (~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 β-xylosidases. However, enzyme immobilization could be improved by lowering the glutaraldehyde loading used to activate the alginate beads, resulting in improved hydrolysis efficacy (~65% xylooligomer conversion). Enzyme immobilization improved enzyme thermostability (endoxylanase and β-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.
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Subject | |
Genre | |
Type | |
Language |
eng
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Date Available |
2019-06-17
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Provider |
Vancouver : University of British Columbia Library
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Rights |
CC BY 4.0
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DOI |
10.14288/1.0379461
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URI | |
Affiliation | |
Citation |
Materials 11 (10): 2005 (2018)
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Publisher DOI |
10.3390/ma11102005
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Peer Review Status |
Reviewed
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Scholarly Level |
Faculty
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Rights URI | |
Aggregated Source Repository |
DSpace
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Item Media
Item Citations and Data
Rights
CC BY 4.0