Properties of cellulose-binding modules in endoglucanase F from Fibrobacter succinogenes S85 by means of surface plasmon resonance

• Published in: FEMS microbiology letters 2002-09, Vol.214 (2), p.277-281
• Main Authors: Mitsumori, M, Xu, L, Kajikawa, H, Kurihara, M
• Format: Article
• Language: English
• Subjects: Bacteria - enzymology; Bacteriology; Binding sites; Biological and medical sciences; Calcium; Calcium - pharmacology; Carboxymethylcellulose; Carboxymethylcellulose Sodium - metabolism; Cellooligosaccharides; Cellulase - metabolism; Cellulose; Cellulose fibers; Cellulose‐binding module; endo-1,4-beta-glucanase; Endoglucanase; Fibrobacter succinogenes; Fundamental and applied biological sciences. Psychology; Magnesium - pharmacology; Microbiology; Modules; Morphology, structure, chemical composition; Oligosaccharides - pharmacology; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains; recombinant proteins; Recombinant Proteins - metabolism; Resonance; Rumen bacterium; Surface Plasmon Resonance
• ISSN: 0378-1097; 1574-6968
• DOI: 10.1111/j.1574-6968.2002.tb11359.x

Properties of the recombinant proteins derived from Fibrobacter succinogenes endoglucanase F (EGF), AD2 and AD4, were characterized using surface plasmon resonance. Because AD2, which contains two reiterated regions, showed stronger affinity to immobilized carboxymethylcellulose (CMC) than did AD4, which contains only the first reiterated region, it has been assumed that the reiterated regions of EGF are cellulose-binding modules. While calcium enhanced the binding of AD2 to the immobilized CMC, it did not enhance the binding of AD4. Moreover, the results obtained from experiments using cellooligosaccharides showed that the binding sites of AD4 and AD2 span approximately four and nine glucosyl units, respectively.