Specific adhesion and hydrolysis of cellulose by intact Escherichia coli expressing surface anchored cellulase or cellulose binding domains

• Published in: Bio/technology (New York, N.Y. 1983) Vol. 11; no. 4; pp. 491 - 495
• Main Authors: Francisco, J A, Stathopoulos, C, Warren, R A, Kilburn, D G, Georgiou, G
• Format: Journal Article
• Language: English
• Published: United States 01.04.1993
• Subjects: Actinomycetales - enzymology; Amino Acid Sequence; Bacterial Adhesion; Bacterial Outer Membrane Proteins - genetics; Base Sequence; beta-Glucosidase - genetics; beta-Glucosidase - metabolism; Binding Sites - genetics; Cell Membrane - enzymology; Cellulase - metabolism; Cellulose - metabolism; Escherichia coli - genetics; Escherichia coli - physiology; Gene Expression; Glucan 1,3-beta-Glucosidase; Hydrolysis; Lipoproteins - genetics; Microscopy, Electron, Scanning; Microscopy, Fluorescence; Molecular Sequence Data; Papain - metabolism; Recombinant Fusion Proteins - metabolism

The entire Cex exoglucanase from Cellulomonas fimi and the Cex Cellulose Binding Domain (CBDCex) were expressed in Escherichia coli as fusions to an Lpp-OmpA hybrid which had been shown earlier to direct a heterologous protein to the cell surface. Both Cex and CBDCex were readily localized on the ce...