@inbook {3835,
	title = {Cellulose-binding domains - Versatile affinity tags for inexpensive large-scale purification, concentration, and immobilization of fusion proteins},
	booktitle = {Enzyme Engineering Xiii},
	series = {Annals of the New York Academy of Sciences},
	volume = {799},
	year = {1996},
	note = {ISI Document Delivery No.: BK03HTimes Cited: 6Cited Reference Count: 15Proceedings Paper13th International Enzyme Engineering ConferenceOCT 15-20, 1995SAN DIEGO, CALIFORNIAEngn Fdn, New York2 EAST 63RD ST, NEW YORK, NY 10021 USA},
	pages = {418-424},
	publisher = {New York Acad Sciences},
	organization = {New York Acad Sciences},
	address = {New York},
	keywords = {ESCHERICHIA-COLI, FIMI},
	isbn = {0077-89230-89766-981-9},
	url = {<Go to ISI>://000070949000067},
	author = {Tomme, P. and Gilkes, N. R. and Guarna, M. M. and Haynes, C. A. and Hasenwinkle, D. and Jervis, E. and Johnson, P. and McIntosh, L. and Warren, R. A. J. and Kilburn, D. G.},
	editor = {Dordick, J. S. and Russell, A. J.}
}
@article {3621,
	title = {Probing the role of tryptophan residues in a cellulose-binding domain by chemical modification},
	journal = {Protein Science},
	volume = {5},
	number = {11},
	year = {1996},
	note = {ISI Document Delivery No.: VQ786Times Cited: 41Cited Reference Count: 34},
	month = {Nov},
	pages = {2311-2318},
	type = {Article},
	abstract = {The cellulose-binding domain (CBDCex) of the mixed function glucanase-xylanase Cex from Cellulomonas fimi contains five tryptophans, two of which are located within the p-barrel structure and three exposed on the surface (Xu GY et al., 1995, Biochemistry 34:6993-7009). Although all five tryptophans can be oxidized by N-bromosuccinimide (NBS), stopped-flow measurements show that three tryptophans react faster than the other two. NMR analysis during the titration of CBDCex with NBS shows that the tryptophans on the surface of the protein are fully oxidized before there is significant reaction with the two buried tryptophans. Additionally, modification of the exposed tryptophans does not affect the conformation of the backbone of CBDCex, whereas complete oxidation of all five tryptophans denatures the polypeptide. The modification of the equivalent of one and two tryptophans by NBS reduces binding of CBDCex to cellulose by 70\% and 90\%, respectively. This confirms the direct role of the exposed aromatic residues in the binding of CBDCex to cellulose. Although adsorption to cellulose does afford some protection against NBS, as evidenced by the increased quantity of NBS required to oxidize all of the tryptophan residues, the polypeptide can still be oxidized completely when adsorbed. This suggests that, whereas the binding appears to be irreversible overall [Ong E et al., 1989, Bio/Technology 7:604-607], each of the exposed tryptophans interacts reversibly with cellulose.},
	keywords = {absorbance spectroscopy, ACTIVE-SITE, CELLOBIOHYDROLASE-I, cellulose-binding, ENDOGLUCANASE, ESCHERICHIA-COLI, FIMI, fluorescence spectroscopy, N-bromosuccinimide, NMR, NUCLEAR-MAGNETIC-RESONANCE, SCHIZOPHYLLUM-COMMUNE, SPECTROSCOPY, TRICHODERMA-REESEI, XYLANASE-A},
	isbn = {0961-8368},
	url = {<Go to ISI>://A1996VQ78600017},
	author = {Bray, M. R. and Johnson, P. E. and Gilkes, N. R. and McIntosh, L. P. and Kilburn, D. G. and Warren, R. A. J.}
}
@article {3144,
	title = {TECHNOLOGY FOR REGENERABLE BIOSENSOR PROBES BASED ON ENZYME CELLULOSE-BINDING DOMAIN CONJUGATES},
	journal = {Biotechnology Progress},
	volume = {10},
	number = {4},
	year = {1994},
	note = {ISI Document Delivery No.: PC847Times Cited: 9Cited Reference Count: 39},
	month = {Jul-Aug},
	pages = {433-440},
	type = {Article},
	abstract = {The application of enzyme-based biosensors for on-line bioprocess monitoring and control has been slowed by problems relating to the in situ sterilizability of the probe and the stability of the enzyme component. A novel technology with the potential to address both of these difficulties is presented here, The approach is based on the reversible immobilization of enzymes conjugated with the cellulose binding domain (CBD) of cellulases from Cellulomonas fimi. A regenerable biosensor electrode can be configured with a cellulose matrix onto which the enzyme-CBD conjugate can be repeatedly loaded (bound by the CBD) and subsequently eluted by perfusing the cellulose matrix with the appropriate solution. Glucose oxidase (GOx) conjugated to CBD with glutaraldehyde was used in an experimental glucose biosensor to demonstrate the feasibility of multiple cycles of loading and elution of the conjugate. Michaelis-Menten enzyme kinetics provided an empirical model for the calibration of the experimental biosensor. The development of a computer-controlled prototype glucose biosensor and a fermentation monitoring system based on this approach is discussed.},
	keywords = {CLONING, electrode, ESCHERICHIA-COLI, EXOGLUCANASE, FIMI, GENE, GLUCOSE-OXIDASE, IMMOBILIZATION, ONLINE DETERMINATION, SEQUENCE},
	isbn = {8756-7938},
	url = {<Go to ISI>://A1994PC84700014},
	author = {Phelps, M. R. and Hobbs, J. B. and Kilburn, D. G. and Turner, R. F. B.}
}
