Characterization of a Neocallimastix patriciarum cellulase cDNA (celA) homologous to Trichoderma reesei cellobiohydrolase II

Article Abstract:

Cellulase A (CELA), encoded by cellulase cDNA from the rumen fungus Neocallimastix patriciarum is structurally similar to cellobiohydrolase II from the aerobic fungus Trichoderma reesei. Nucleotide sequence analysis shows that CELA has a cellulose-binding region at the N-terminus and a catalytic region at the C-terminus separated by an Asn-rich linker. Removal of the N-terminal region reduces cellulose-binding activity. CELA is located in the periplasmic region when expressed in Escherichia coli, suggesting that the signal sequence is functional in E. coli.

Analysis, Enzymes, Nucleotide sequence, Base sequence, Proteins, Protein structure, Enzyme structure-activity relationships

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Two cellulases, CelA and CelC, from the polycentric anaerobic fungus Orpinomyces strain PC-2 contain N-terminal docking domains for a cellulase-hemicellulase complex

Article Abstract:

A research was conducted to investigate the cloning and sequencing of cDNAs encoding similar cellulases of Orpinomyces sp. strain PC-2 and the characterization of the cellulases obtained by expression in Escherichia coli. Enzyme activities were determined in a sodium phosphate solution. The nucleotide sequences of the cellulases were assigned accession numbers in the GenBank database. Results showed that the cellulases depicted structural similarities with each other and that their sequences were dissected into several region.

Anaerobic bacteria, Molecular genetics

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Three Neocallimastix patriciarum esterases associated with the degradation of complex polysaccharides are members of a new family of hydrolases

Article Abstract:

Research has identified three esterase enzymes in the anaerobic ruminal fungus Neocallimastix patriciarum which belong to a new family of hydrolases. Deoxyribonucleic acid (DNA) sequence analysis using a cDNA expression library was performed using beta-naphthyl acetate and a model cinnamoyl ester compound. Four esterase genes were identified. Two, designated BnaA and BnaC, tested positive for acetylxylan esterase activity.

Genetic aspects, Esterases, Enzymatic analysis

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