CLONING AND EXPRESSION OF A BETA-1,4-ENDOGLUCANASE GENE FROM CELLULOMONAS SP CE1B7 IN ESCHERICHIA-COLI, PURIFICATION CHARACTERIZATION OF THE RECOMBINANT ENZYME
L. Fulop et al., CLONING AND EXPRESSION OF A BETA-1,4-ENDOGLUCANASE GENE FROM CELLULOMONAS SP CE1B7 IN ESCHERICHIA-COLI, PURIFICATION CHARACTERIZATION OF THE RECOMBINANT ENZYME, FEMS microbiology letters, 145(3), 1996, pp. 355-360
A gene library of a newly isolated Cellulomonas sp. strain was constru
cted in Escherichia coli and clones were screened for endoglucanase ac
tivity using dye-labelled carboxymethylcellulose. Seventeen clones wer
e isolated that carried DNA inserts coding for endoglucanase enzymes.
Of the 17 clones, one carrying the gene cegA, was further characterize
d. The recombinant endoglucanase was purified by FPLC. The endoglucana
se was active against carboxymethylcellulose, lichenin and also degrad
ed crystalline cellulose and birchwood xylan. The molecular mass of th
e enzyme (36 kDa), and its pH (7.4) and temperature (35 degrees C) opt
ima were determined.