Cited 0 time in
- Thermostable β-glycosidase-CBD fusion protein for biochemical analysis of cotton scouring efficiency = CBD융합단백질을 이용한 생화학적 표면분석기술
- Jae-Seok Ha; Y M Lee; Su Lim Choi; Jae Jun Song; C S Shin; J H Kim; Seung Goo Lee
- Bibliographic Citation
- Journal of Microbiology and Biotechnology, vol. 18, no. 3, pp. 443-448
- Publication Year
- 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 β-glycosidase (BglA) from Thermus caldophilus was found to be most appropriate, showing a higher applicability and stability than GFP, DsRed2, or a tetrameric β-glucuronidase (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.
- β-glycosidase; biochemical analysis; cellulose binding domain; cotton scouring; fusion protein; thermus caldophilus
- South Korea
- Appears in Collections:
- Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
Division of Biomaterials Research > Synthetic Biology and Bioengineering Research Center > 1. Journal Articles
- Files in This Item:
Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.