A multifunctional hybrid glycosyl hydrolase discovered in an uncultured microbial consortium from ruminant gut
| Autor: | Paul Dupree, Dan E. Robertson, Brian Steer, Florence Goubet, Chris S. Lyon, Nisha Palackal, Jay M. Short, Peter Luginbuhl, Geoffrey P. Hazlewood, John L. Macomber, Seema Zaidi |
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| Rok vydání: | 2006 |
| Předmět: |
Rumen
Glycoside Hydrolases Molecular Sequence Data Multifunctional Enzymes Biology Applied Microbiology and Biotechnology Mannans chemistry.chemical_compound Industrial Microbiology Multienzyme Complexes Hydrolase Animals Glycosyl Glucans Mannan Glucan Gene Library chemistry.chemical_classification Base Sequence General Medicine Sequence Analysis DNA Glucanase Enzyme chemistry Biochemistry Xylanase Mutagenesis Site-Directed Cattle Xylans Biotechnology |
| Zdroj: | Applied microbiology and biotechnology. 74(1) |
| ISSN: | 0175-7598 |
| Popis: | A unique multifunctional glycosyl hydrolase was discovered by screening an environmental DNA library prepared from a microbial consortium collected from cow rumen. The protein consists of two adjacent catalytic domains. Sequence analysis predicted that one domain conforms to glycosyl hydrolase family 5 and the other to family 26. The enzyme is active on several different beta-linked substrates and possesses mannanase, xylanase, and glucanase activities. Site-directed mutagenesis studies on the catalytic residues confirmed the presence of two functionally independent catalytic domains. Using site-specific mutations, it was shown that one catalytic site hydrolyzes beta-1,4-linked mannan substrates, while the second catalytic site hydrolyzes beta-1,4-linked xylan and beta-1,4-linked glucan substrates. Polysaccharide Analysis using Carbohydrate gel Electrophoresis (PACE) also confirmed that the enzyme has discrete domains for binding and hydrolysis of glucan- and mannan-linked polysaccharides. Such multifunctional enzymes have many potential industrial applications in plant processing, including biomass saccharification, animal feed nutritional enhancement, textile, and pulp and paper processing. |
| Databáze: | OpenAIRE |
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