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Immobilization and characterization of a thermostable β-xylosidase to generate a reusable biocatalyst

Paper ID Volume ID Publish Year Pages File Format Full-Text
18339 42719 2006 9 PDF Available
Title
Immobilization and characterization of a thermostable β-xylosidase to generate a reusable biocatalyst
Abstract

The thermostable β-xylosidase from Sulfolobus solfataricus, expressed in Escherichia coli, was immobilized by entrapment into alginate with full recovery of activity and tested for xylose production from xylan hydrolysates. Since the recombinant activity was also cell bound, alginate beads entrapping E. coli whole cells were also prepared. The immobilized preparations exhibited higher thermostability at 90 °C compared to their free counterparts. The half-lives of the immobilized enzyme and cells were 21 and 23 h, respectively, while half of the inactivation was reached after 10 and 11.5 h for free enzyme and whole cells. Interestingly, thermophilicity increased from 85 up to 100 °C and the optimal pH shifted to higher values for immobilized preparations. Results obtained from xylo-oligosaccharides hydrolysis in subsequent batch experiments of recycling, indicated that the immobilized enzyme had good operational stability, retaining 84% of its initial activity after four cycles.Here we report on the immobilization of the β-xylosidase into alginate and its characterization.

Keywords
Alginate; Immobilization; Xylose; β-Xylosidase
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Immobilization and characterization of a thermostable β-xylosidase to generate a reusable biocatalyst
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 6, 3 October 2006, Pages 1205–1213
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us