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Comparative Characterization of a Bifunctional endo-1,4-β-Mannanase/ 1,3-1,4-β-glucanase and its Individual Domains

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A fusion gene isolated from a microbial metagenome encodes a N-terminal endo-1,4-β-mannanase and a Cterminal 1,3-1,4-β-glucanase,. The full-length gene and the individual N- and C-domains were separately cloned and expressed in E coli. The purified whole enzyme hydrolyzed glucomannan, galactomannan, and β-glucan with Km and kcat values 2.2, 2.6, 3.6 mg/ml, and 302, 130, 337 min -1 , respectively. The hydrolysis of β-glucan by the C domain enzyme decreased significantly with added glucomannan to the reaction, suggesting inhibition effect. Analogous result was not observed with the N domain enzyme when β-glucan was added to the reaction. The whole enzyme did not show improvement of efficiency compared to the individual or additive total hydrolysis of the two domain enzymes using single or mixed substrates.
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Keywords: 1; 3-1; 4-β-glucanase; bifunctional enzyme; endo-β-mannanase; metagenomic library; β-glucanase; β-mannanase

Document Type: Research Article

Publication date: May 1, 2013

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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