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Updated: Jul 10, 2026
A High Throughput Screen for Biomining Cellulase Activity from Metagenomic Libraries
Published on: February 2, 2011
Cloning of Clostridium cellulovorans endo-1,4-beta-glucanase genes
O Shoseyov1, T Hamamoto, F Foong
1Department of Biochemistry and Biophysics, University of California, Davis 95616.
Abstract:
A Clostridium cellulovorans lambda gt11 gene bank was screened for endo-1,4-beta-glucanase [EC 3.2.1.4, EGase, Carboxy Methyl Cellulase (CMCase)] genes using a chromogenic substrate. Three genes (engA, engB, and engC) were isolated. The engB expressed the most active CMCase. The engA encoded a bifunctional enzyme that displayed endo-1,4-beta-glucanase and beta-glucosidase activities. The three recombinant glucanases, when expressed in Escherichia coli, were partially degraded into multiform active enzymes as evidenced by their SDS-PAGE-CMC zymograms. None of the clones could degrade crystalline cellulose, thus supporting the hypothesis that the integrity of the C. cellulovorans cellulase complex was essential for its 'true cellulase' activity.
