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

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.

authors

Quentin M,Ebbelaar M,Derksen J,Mariani C,van Der Valk H

doi

10.1007/s00253-002-0937-4

subject

Has Abstract

pub_date

2002-04-01 00:00:00

pages

658-62

issue

5

eissn

0175-7598

issn

1432-0614

journal_volume

58

pub_type

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