Abstract
A family 26, glycoside hydrolase (GH26) named lichenase of the molecular size 30 kDa fromClostridium thermocellum previously cloned into an expression vector pET21a was over-expressed inEscherichia coli BL-21 cells and was purified to homogeneity by a single step purification method using immobilised metal ion affinity-chromatography. The purified enzyme showed no activity towards soluble substrates such as carboxymethyl cellulose, hydroxymethyl cellulose, laminarin, galactomannan or glucomannan. However, unlike other members of the family GH26, the enzyme lichenase showed high activity towards lichenan and β-glucan and was highly specific endo acting β-1,3-1,4-glucanase. Quantitative affinity-gel electrophoresis on native-PAGE showed that lichenase binds only glucomannan (with aKa of 41.3 C−1) and not lichenan or β-glucan.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
