Cloning and characterization of a modular GH5 β-1,4-mannanase with high specific activity from the fibrolytic bacterium Cellulosimicrobium sp. strain HY-13
| Autor: | Dong-Ha Shin, Su-Jin Ham, Kwang-Hee Son, Yi-Joon Kim, Hyunju Lee, Han-Young Cho, Do Young Kim, Young Ha Rhee, Ji Hoon Kim, Ho-Yong Park |
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| Rok vydání: | 2011 |
| Předmět: |
Environmental Engineering
Cellulosimicrobium Molecular Sequence Data Bioengineering Curdlan Biology Polysaccharide medicine.disease_cause Galactans Catalysis Chromatography Affinity Mannans chemistry.chemical_compound Chitin Actinomycetales Mannosidases Plant Gums medicine Mannobiose Escherichia coli Animals Cloning Molecular Oligochaeta Waste Management and Disposal Mannan chemistry.chemical_classification Base Sequence Renewable Energy Sustainability and the Environment Temperature General Medicine Sequence Analysis DNA Hydrogen-Ion Concentration Recombinant Proteins chemistry Biochemistry Locust bean gum Electrophoresis Polyacrylamide Gel |
| Zdroj: | Bioresource technology. 102(19) |
| ISSN: | 1873-2976 |
| Popis: | The gene (1272-bp) encoding a β-1,4-mannanase from a gut bacterium of Eisenia fetida , Cellulosimicrobium sp. strain HY-13 was cloned and expressed in Escherichia coli . The recombinant β-1,4-mannanase (rManH) was approximately 44.0 kDa and has a catalytic GH5 domain that is 65% identical to that of the Micromonospora sp. β-1,4-mannosidase. The enzyme exhibited the highest catalytic activity toward mannans at 50 °C and pH 6.0. rManH displayed a high specific activity of 14,711 and 8498 IU mg −1 towards ivory nut mannan and locust bean gum, respectively; however it could not degrade the structurally unrelated polysaccharides, mannobiose, or p -nitrophenyl sugar derivatives. rManH was strongly bound to ivory nut mannan, Avicel, chitosan, and chitin but did not attach to curdlan, insoluble oat spelt xylan, lignin, or poly(3-hydroxybutyrate). The superior biocatalytic properties of rManH suggest that the enzyme can be exploited as an effective additive in the animal feed industry. |
| Databáze: | OpenAIRE |
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