Description of a cellulose-binding domain and a linker sequence from Aspergillus fungi

被引：0
|
作者：
M. Quentin
M. Ebbelaar
J. Derksen
C. Mariani
H. van der Valk
机构：
[1] Department of Fibre and Paper Technology,
[2] ATO BV,undefined
[3] PO Box 17,undefined
[4] 6700 AA Wageningen,undefined
[5] The Netherlands,undefined
[6] Department of Pharmaceutical Biology,undefined
[7] University of Groningen,undefined
[8] PO Box 72,undefined
[9] 9700 AB Groningen,undefined
[10] The Netherlands,undefined
[11] Department of Experimental Botany,undefined
[12] Catholic University of Nijmegen,undefined
[13] Toernooiveld 1,undefined
[14] 6525 ED Nijmegen,undefined
[15] The Netherlands,undefined
来源：
Applied Microbiology and Biotechnology | 2002年 / 58卷
关键词：
Cellulose; Glutathione; Serine; Molecular Mass; Fusion Protein;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
A family I cellulose-binding domain (CBD) and a serine- and threonine-rich linker peptide were cloned from the fungi Aspergillus japonicus and Aspergillus aculeatus. A glutathione S-transferase (GST) fusion protein comprising GST and a peptide linker with the CBD fused to its C-terminus, was expressed in Escherichia coli. The renatured GST-CBD recovered from inclusion bodies had a molecular mass of 36.5 kDa which agrees with the 29 kDa of the GST plus the calculated 7.5 kDa of the linker with the CBD. The isolated GST-CBD protein adsorbed to both bacterial microcrystalline cellulose and carboxymethyl cellulose. Deletion of the linker peptide caused a decrease in cellulose adsorbance and a higher sensitivity to protease digestion.
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页码：658 / 662
页数：4
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