Catalytic properties of the cellulose-binding endoglucanase F from Fibrobacter succinogenes S85

• Published in: Applied and Environmental Microbiology Vol. 63; no. 6; pp. 2449 - 2453
• Main Authors: Malburg, S.R.C. (University of California, Davis, CA.), Malburg, L.M. Jr, Liu, T, Iyo, A.H, Forsberg, C.W
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for Microbiology 01.06.1997
• Subjects: ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; Amino Acid Sequence; Animals; BACTERIA; Bacteriology; Binding Sites; Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; Catalysts; CELLULASE; Cellulase - chemistry; Cellulase - genetics; Cellulase - metabolism; Cellulose - metabolism; CELULASA; COMPOSICION QUIMICA; COMPOSITION CHIMIQUE; Enzymes; Fibrobacter succinogenes; Fundamental and applied biological sciences. Psychology; Genes, Bacterial; Gram-Negative Anaerobic Bacteria - enzymology; Gram-Negative Anaerobic Bacteria - genetics; MICROORGANISME DU RUMEN; MICROORGANISMOS DEL RUMEN; Miscellaneous; Mission oriented research; Molecular Sequence Data; Molecular Weight; Restriction Mapping; Rumen - microbiology; SECUENCIA NUCLEOTIDICA; Sequence Homology, Amino Acid; SEQUENCE NUCLEOTIDIQUE; Fibrobacter succinogenes; Enzyme; Sequence alignment; Cellulose; Homology; Gene expression; Bacteroidaceae; Binding capacity; Enzymatic activity; Glycosidases; Substrate specificity; Bacteria; Hydrolases; Molecular domain; Aminoacid sequence
• ISSN: 0099-2240; 1098-5336
• DOI: 10.1128/aem.63.6.2449-2453.1997

The celF gene from the predominant cellulolytic ruminal bacterium Fibrobacter succinogenes encodes a 118.3-kDa cellulose-binding endoglucanase, endoglucanase F (EGF). This enzyme possesses an N-terminal cellulose-binding domain and a C-terminal catalytic domain. The purified catalytic domain displayed an activity profile typical of an endoglucanase, with high catalytic activity on carboxymethyl cellulose and barley beta-glucan. Immunoblotting of EGF and the formerly characterized endoglucanase 2 (EG2) from F. succinogenes with antibodies prepared against each of the enzymes demonstrated that EGF and EG2 contain cross-reactive epitopes. This data in conjunction with evidence that the proteins are the same size, share a 19-residue internal amino acid sequence, possess similar catalytic properties, and both bind to cellulose allows the conclusion that celF codes for EG2