Abstract:
: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.
journal_name
Appl Microbiol Biotechnoljournal_title
Applied microbiology and biotechnologyauthors
Quentin M,Ebbelaar M,Derksen J,Mariani C,van Der Valk Hdoi
10.1007/s00253-002-0937-4subject
Has Abstractpub_date
2002-04-01 00:00:00pages
658-62issue
5eissn
0175-7598issn
1432-0614journal_volume
58pub_type
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