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Thermostable ${\beta}$-Glycosidase-CBD Fusion Protein for Biochemical Analysis of Cotton Scouring Efficiency  

Ha, Jae-Seok (Systems Microbiology, Research Center, KRIBB)
Lee, Young-Mi (Systems Microbiology, Research Center, KRIBB)
Choi, Su-Lim (Systems Microbiology, Research Center, KRIBB)
Song, Jae-Jun (Molecular Bioprocess Research Center, KRIBB)
Shin, Chul-Soo (Department of Biotechnology, Yonsei University)
Kim, Ju-Hea (Textile Ecology Laboratory, KITECH)
Lee, Seung-Goo (Systems Microbiology, Research Center, KRIBB)
Publication Information
Journal of Microbiology and Biotechnology / v.18, no.3, 2008 , pp. 443-448 More about this Journal
Abstract
Multidomain proteins for the biochemical analysis of the scouring efficiency of cotton fabrics were constructed by the fusion of a reporter moiety in the N-terminal and the cellulose binding domain (CBD) in the C-terminal. Based on the specific binding of the CBD of Cellulomonas fimi exoglucanase (Cex) to crystalline cellulose (Avicel), the reporter protein is guided to the cellulose fibers that are increasingly exposed as the scouring process proceeds. Among the tested reporter proteins, a thermostable ${\beta}$-glycosidase (BglA) from Thermus caldophilus was found to be most appropriate, showing a higher applicability and stability than GFP, DsRed2, or a tetrameric ${\beta}$-glycosidase (GUS) from Escherichia coli, which were precipitated more seriously during the expression and purification steps. When cotton fabrics with different scouring levels were treated with the BglA-CBD and incubated with X-Gal as the chromogenic substrate, an indigo color became visible within 2 h, and the color depth changed according to the conditions and extent of the scouring.
Keywords
Cotton scouring; biochemical analysis; fusion protein; cellulose binding domain; Thermus caldophilus${\beta}$-glycosidase;
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Times Cited By Web Of Science : 0  (Related Records In Web of Science)
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