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Characterization of a recombinant β-glucosidase from the thermophilic bacterium Caldicellulosiruptor saccharolyticus

Paper ID Volume ID Publish Year Pages File Format Full-Text
21748 43238 2009 5 PDF Available
Title
Characterization of a recombinant β-glucosidase from the thermophilic bacterium Caldicellulosiruptor saccharolyticus
Abstract

A recombinant β-glucosidase from Caldicellulosiruptor saccharolyticus DSM 8903 with a specific activity of 13 U/mg was purified by heat treatment and His-Trap affinity chromatography and identified as a single 54 kDa band on SDS-PAGE. The molecular mass of the native enzyme was 108 kDa as a dimer by gel filtration. β-Glucosidase showed optimum activity at pH 5.5 and 70 °C for p-nitrophenyl (pNP)-β-d-glucopyranoside. The half-lives of the enzyme at 60, 70, and 80 °C were 250, 24.3, and 0.4 h, respectively. The enzyme exhibited catalytic efficiency and specific activity for pNP-β-d-fucopyranoside, pNP-β-d-glucopyranoside, and pNP-β-d-galactopyranoside in decreasing order among aryl-β-glycosides, but not for aryl-α-glycosides. Cello-oligosaccharides from n = 2 to 5 as substrates using 4 mM each sugar and 3 U/mg of enzyme were completely hydrolyzed to glucose at 70 °C within 16 h.

Keywords
Caldicellulosiruptor saccharolyticus; Cello-oligosaccharides; Characterization; β-Glucosidase; Saccharification; Thermostable enzyme
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Characterization of a recombinant β-glucosidase from the thermophilic bacterium Caldicellulosiruptor saccharolyticus
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 108, Issue 1, July 2009, Pages 36–40
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